Peripheral Membrane Proteins

  • Barbara A. Seaton
  • Mary F. Roberts


The founding principle behind structural biology is that form equals function. Nowhere is this relation more apparent than in proteins that operate in environments in which aqueous and lipophilic phases meet. This biphasic environment strongly influences both the structure and function of these proteins. Membrane proteins can be classified as integral or peripheral, depending upon the nature of the protein-membrane association. For proteins in the former category, the membrane is an integral part of their structures, which are greatly perturbed by disruption of the membrane by detergents. The extent of interaction with the lipid bilayer is usually obvious by simple inspection of the protein structure because of what is known about lipid physical chemistry, i.e., that there is a large energy cost to burying uncompensated polar or charged protein residues in a strongly hydrophobic milieu. For example, the membrane-embedded portions of transmembrane proteins, such as bacterial reaction centers and porins, are localized by the extensive hydrophobic regions, which are frequently bordered by aromatic side-chains, found on the surfaces of these proteins. For these transmembrane proteins, whose functional roles are to transfer energy or substances from one aqueous pool to another across a nonaqueous barrier, the membrane serves to organize the protein structure. In contrast to integral membrane proteins, those classified as peripheral can be released from their membrane attachment through gentler means, without disruption of either membrane or protein structure.


Annexin Versus Bacillus Cereus Phosphatidic Acid Pancreatic Lipase Interfacial Activation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Abousalham A, Riviere M, Teissere M, Verger R (1993): Improved purification and biochemical characterization of phospholipase D from cabbage. Biochim Biophys Acta 1158:1–7PubMedGoogle Scholar
  2. Ackermann EJ, Kempner ES, Dennis EA (1994): Ca2+-independent cytosolic phospholipase A2 from macrophage-like P388D1 cells. Isolation and characterization.J Biol Chem 269:9227–9233PubMedGoogle Scholar
  3. Ames JB, Porumb T, Tanaka T, Ikura M, Stryer L (1995): Amino-terminal myristoylation induces cooperative calcium binding to recoverin.J Biol Chem 270:4526–4533PubMedGoogle Scholar
  4. Ames JB, Tanaka T, Stryer L, Ikura M (1994): Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch. Biochemistry 33:10743–10753PubMedGoogle Scholar
  5. Andree HAM, Stuart MCA, Hermens W, Reutelingsperger CPM, Hemker HC, Frederik PM, Willems GM (1992): Clustering of lipid-bound annexin-V may explain its anticoagulant effect.J Biol Chem 267:17907–17912PubMedGoogle Scholar
  6. Artursson E, Puu G (1992): A phosphatidylinositol-specific phospholipase C from Cytophaga: Production, purification, and properties. Can J Microbiol 38:1334–1337Google Scholar
  7. Berridge MJ (1986): Phosphoinositides and receptor mechanisms. In: Receptor Biochemistry and Methodology, Putney JW, ed. New York: Alan LissGoogle Scholar
  8. Bewley MC, Boustead CM, Walker JH, Waller DA, Huber R (1993): Structure of chicken annexin V at 2.25-Å resolution. Biochemistry 32:3923–3929PubMedGoogle Scholar
  9. Billah MM, Anthes JC (1990): The regulation and cellular functions of PC hydrolysis. Biochem J 269:281–291PubMedGoogle Scholar
  10. Blackwood RA, Ernst JD (1990): Characterization of Ca2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins. Biochem J 266:195–200PubMedGoogle Scholar
  11. Blow D (1991): Lipases reach the surface. Nature 351:444–445PubMedGoogle Scholar
  12. Borowski M, Furie BC, Bauminger S, Furie B (1986): Prothrombin requires two sequential metal-dependent conformational transition to bind phospholipid. J Biol Chem 261:14969–14975PubMedGoogle Scholar
  13. Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C (1994): Horse pancreatic lipase. The crystal structure refined at 2.3 Å resolution.J Mol Biol 238:709–732PubMedGoogle Scholar
  14. Brady L, Brzozowksi AM, Derewenda ZS, Dodson E, Dodson G, Tolley S, Turkenberg JP, Christiansen L, Huge-Jensen B, Norskov L, Thim L, Menge U (1990): A serine protease forms the catalytic centre of a triacylglycerol lipase. Nature 343:767–770PubMedGoogle Scholar
  15. Brisson A, Mosser G, Huber R (1991): Structure of soluble and membrane-bound human annexin V.J Mol Biol 220:199–203PubMedGoogle Scholar
  16. Brunie S, Bolin J, Gewirth D, Sigler PB (1985): The refined crystal structure of dimeric phospholipase A2 at 2.5 Å. Access to a shielded catalytic center.J Biol Chem 260:9742–9749PubMedGoogle Scholar
  17. Brzozowski AM, Derewenda U, Derewenda ZS, Dodson GG, Lawson DM, Turkenberg JP, Bjorkling F, Huge-Jensen B, Patkar SA, Thim L (1991): A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351:491–494PubMedGoogle Scholar
  18. Camilli A, Goldfine H, Portnoy DA (1991): Listeria monocytogenes mutants lacking Pi-specific phospholipase C are equivalent. J Exp Med 173:751–754PubMedGoogle Scholar
  19. Clark JD, Lin L, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL (1991) A novel arachidonic acid-selective cytosolic PLA2 contains a Ca-dependent translocation domain with homology to PKC and GAP. Cell 65:1043–1051PubMedGoogle Scholar
  20. Clark MA, Shorr RGL, Bomalski JS (1986): Antibodies prepared to Bacillus cereus phospholipase C crossreact with a phosphatidylcholine preferring phospholipase C in mammalian cells. Biochem Biophys Res Commun 140:114–119PubMedGoogle Scholar
  21. Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA (1993): Rat annexin V crystal structure: Ca2+-induced conformational changes. Science 261:1321–1324PubMedGoogle Scholar
  22. Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA (1992): Annexin-V forms calcium dependent trimeric units on phospholipid vesicles. FEBS Lett 314:159–162PubMedGoogle Scholar
  23. Creutz CE (1992): The annexins and exocytosis. Science 258:924–931PubMedGoogle Scholar
  24. Crumpton MJ, Dedman JR (1990): Protein terminology tangle. Nature 345:212PubMedGoogle Scholar
  25. De Haas GH, Bonsen PPM, Pieterson WA, Van Deenen LLM (1971): Studies on phospholipase A2 and its zymogen from porcine pancreas. Biochim Biophys Acta 239:252–266PubMedGoogle Scholar
  26. Demange P, Voges D, Benz J, Liemann S, Göttig P, Berendes R, Burger A, Huber R (1994): Annexin V: the key to understanding ion selectivity and voltage regulation? Trends Biochem Sci 19:272–276PubMedGoogle Scholar
  27. Dennis EA (1994): Diversity of group types, regulation, and function of phospholipase A2. J Biol Chem 269:13057–13060PubMedGoogle Scholar
  28. Derewenda U, Brzozowski AM, Lawson DM, Derewenda ZS (1992a): Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase. Biochemistry 31:1532–1541PubMedGoogle Scholar
  29. Derewenda ZS, Derewenda U, Dodson GG (1992b): The crystal and molecular structure of the Rhizomucor miehei triglyceride lipase at 1.9 Â resolution. J Mol Biol 227:818–839PubMedGoogle Scholar
  30. Derewenda U, Swenson L, Green R, Wei Y, Dodson GG, Yamaguchi S, Haas MJ, Derewenda ZS (1994): An unusual buried polar cluster in a family of fungal lipases. Nature Struct Biol 1:36–47PubMedGoogle Scholar
  31. Dijkstra BW, Kalk KH, Hol WGJ, Drenth J (1981): Structure of porcine pancreatic phospholipase A2 at 1.7 Å resolution. J Mol Biol 147:97–123PubMedGoogle Scholar
  32. Dijkstra BW, Renetseder R, Kalk KH, Hol WGJ, Drenth J (1983): Structure of porcine pancreatic phospholipase A2 at 2.6 Å resolution and comparison with bovine phospholipase A2.J Mol Biol 168:163–179PubMedGoogle Scholar
  33. Dizhoor AM, Chen CK, Olshevskaya E, Sinelnikova VV, Phillipov P, Hurley JB (1993): Role of the acylated amino terminus of recoverin in Ca2+-dependent membrane interaction. Science 259:829–832PubMedGoogle Scholar
  34. Dodson GG, Lawson DM, Winkler FK (1992): Structural and evolutionary relationships in lipase mechanism and activation. Faraday Discuss 93:95–105PubMedGoogle Scholar
  35. Evans TC Jr, Nelsestuen GL (1994): Calcium and membrane-binding properties of monomeric and multimeric annexin II. Biochemistry 33:13231–13238PubMedGoogle Scholar
  36. Exton J (1990): Signaling through PC breakdown.J Biol Chem 265:1–4PubMedGoogle Scholar
  37. Ferguson JE, Hanley MR (1992): Phosphatidic acid and lysophosphatidic acid stimulate receptor-regulated membrane currents. Arch Biochem Biophys 297:388–392PubMedGoogle Scholar
  38. Flaherty KM, Zozulya S, Stryer L, McKay DB (1993): Three-dimensional structure of recoverin, a calcium sensor in vision. Cell 75:709–716PubMedGoogle Scholar
  39. Freedman SJ, Furie BC, Furie B, Baleja JD (1995a): Structure of the metal-free τ-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. J Biol Chem 270:7980–7987PubMedGoogle Scholar
  40. Freedman SJ, Furie BC, Furie B, Baleja JD (1995b): Structure of the Ca2+-bound τ-carboxyglutamic acid-rich factor IX. Biochemistry: in pressGoogle Scholar
  41. Fremont DH, Anderson DH, Wilsom IA, Dennis EA, Xuong NH (1993): Crystal structure of phospholipase A2 from Indian cobra reveals a trimeric association. Proc Natl Acad Sci USA 90:342–346PubMedGoogle Scholar
  42. Furie B, Furie BC (1988): The molecular basis of blood coagulation. Cell 53:505–518PubMedGoogle Scholar
  43. Geisow MJ, Walker JH (1986): New proteins involved in cell regulation by Ca2+ and phospholipids. Trends Biol Sci 11:420–423Google Scholar
  44. Goossens ELJ, Reutelingsperger CPM, Jongsma FHM, Kraayenhof R, Hermens W (1995): Annexin V perturbs or stabilises phospholipid membranes in a calcium-dependent manner. FEBS Lett 359:155–158PubMedGoogle Scholar
  45. Gray-Kellor MP, Polans AS, Palczewski K, Detwiler PB (1993): The effect of recoverin-like calcium-binding proteins on the photo response of retinal rods. Neuron 10:523–531Google Scholar
  46. Griffith OH, Volwerk JJ, Kuppe A (1991): Phosphatidylinositol-specific phospholipase C from Bacillus cereus and Bacillus thuringiensis. Melh Enzymol 197:493–502Google Scholar
  47. Grochulski P, Li Y, Schräg JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M (1993): Insights into interfacial activation from an open structure of Candida rugosa lipase.J Biol Chem 268:12843–12847PubMedGoogle Scholar
  48. Hansen S, Hansen LK, Hough E (1992): Crystal structures of phosphate, iodide, and iodate-inhibited phospholipase C from Bacillus cereus and structural investigations of the binding of reaction products and a substrate analogue. J Mol Biol 225:543–549PubMedGoogle Scholar
  49. Hansen S, Hough E, Svensson LA, Wong Y-L, Martin SF (1993): Crystal structure of phospholipase C from Bacillus cereus complexed with a substrate analog. J Mol Biol 234:179–187PubMedGoogle Scholar
  50. Hazen SL, Gross RW (1993): The specific association of a phosphofructokinase isoform with myocardial calcium-independent phospholipase A2.J Biol Chem 268:9892–9900PubMedGoogle Scholar
  51. Head JF (1994): Shedding light on recoverin. Curr Biol 4:64–66PubMedGoogle Scholar
  52. Head JF (1992): A better grip on calmodulin. Curr Biol 2:609–611PubMedGoogle Scholar
  53. Heinz DW, Ryan M, Bullock TL, Griffith OH (1995): Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myoinositol. EMBO J: in pressGoogle Scholar
  54. Hilkman H, de Widt J, Vander Bend R (1991): Phospholipid metabolism in bradykinin-stimulated human fibroblasts. J Biol Chem 266:10344–10350Google Scholar
  55. Hjorth A, Carrière F, Cudrey C, Wöoldike H, Boel E, Lawson DM, Ferrato F, Cambillau C, Dodson GG, Thim L, Verger R (1993): A structural domain (the lid) found in pancreatic lipases is absent in the guinea pig (phospho)lipase. Biochemistry 32:4702–4707PubMedGoogle Scholar
  56. Hoekstra D, Buist-Arkema R, Klappe K, Reutelingsperger CPM (1993): Interaction of annexins with membranes: the N-terminus as a governing parameter as revealed with a chimeric annexin. Biochemistry 32:14194–14202PubMedGoogle Scholar
  57. Hough E, Hansen LK, Birknes B, Jynge K, Hansen S, Hordvik A, Little C, Dodson E, Derewenda Z (1989): High-resolution (1.5 Å) crystal structure of phospholipase C from Bacillus cereus. Nature 338:357–360PubMedGoogle Scholar
  58. Huber R, Berendes R, Burger A, Schneider M, Karshikov A, Luecke H, Römisch J, Pâques E (1992): Crystal and molecular structure of human annexin V after refinement. J Mol Biol 223:683–704PubMedGoogle Scholar
  59. Huber R, Römisch J, Pâques E-P (1990): The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J 9:3867–3974PubMedGoogle Scholar
  60. Ikezawa H, Taguchi T (1981): Phosphatidylinositol-specific phospholipase C from Staphylococcus aureus. Meth Enzymol 71:731–741Google Scholar
  61. Ishizaki J, Hanasaki K, Higashino K, Kishino J, Kibuchi N, Ohara O, Arita H (1994): Molecular cloning of pancreatic group I phospholipase A2 receptor. J Biol Chem 269:5897–5904PubMedGoogle Scholar
  62. Jacobs M, Freedman SJ, Furie BC, Furie B (1994): Membrane binding properties of the factor IX γ-carboxyglutamic acid-rich domain prepared by chemical synthesis. J Biol Chem 269:25494–25501PubMedGoogle Scholar
  63. Jager K, Stieger S, Brodbeck U (1991): Cholinesterase solubilizing factor from Cytophaga sp. is a Pi-specific phospholipase C. Biochem Biophys Acta 1074:45–51PubMedGoogle Scholar
  64. Jalink K, Van Corven EJ, Moolenaar WH (1990): Lysophosphatidic acid, but not phosphatidic acid, is a potent Ca2+-mobilizing stimulus for fibroblasts. Evidence for an extracellular site of action.J Biol Chem 265:12232–12239PubMedGoogle Scholar
  65. Johansen T, Holm T, Guddal PH, Sletten K, Haugli FB, Little C (1988): Cloning and sequencing of the gene encoding the phosphatidylcholine-preferring phospholipase C of Bacillus cereus. Gene 65:293–304PubMedGoogle Scholar
  66. Joseph D, Petsko GA, Karplus M (1990): Anatomy of a conformation-al change: hinged “lid” motion of the triosephosphate isomerase loop. Science 249:1425–1428PubMedGoogle Scholar
  67. Jost M, Weber K, Gerke V (1994): Annexin II contains two types of Ca2+-binding sites. Biochem J 298:553–558PubMedGoogle Scholar
  68. Kaetzel MA, Hazarika P, Dedman JR (1989): Differential tissue expression of three 35 kDa annexin calcium-dependent phospholipid-binding proteins.J Biol Chem 264: 14463–14470PubMedGoogle Scholar
  69. Karshikov A, Berendes R, Burger A, Cavalié, A, Lux HD, Huber R (1992): Annexin V membrane interaction: an electrostatic potential study. Eur Biophys J 20:337–344Google Scholar
  70. Katan M, Kriz RW, Totty N, Meldrum E, Aldape RA, Knopf JL, Parker PJ (1988): Determination of the primary structure of PLC-154 demonstrates diversity of phosphoinositide-specific phospholipase C activities. Cell 54:171–177PubMedGoogle Scholar
  71. Kramer RM, Roberts EF, Manetta J, Putnam JE (1991): The Ca2+-sensitive cytosolic phospholipase A2 is a 100 kDa protein in human monoblast U937.J Biol Chem 266:5268–5272PubMedGoogle Scholar
  72. Kudo I, Murakami M, Hara S, Inoue K (1993): Mammalian non-pancreatic phospholipase A2. Biochim Biophys Acta 1117:217–231Google Scholar
  73. Lawson DM, Brzozowski AM, Rety S, Verma C, Dodson GG (1994): Probing the nature of the substrate binding site in Humicola lanuginosa lipase through X-ray crystallography and intuitive modelling. Prot Engin 7:543–550Google Scholar
  74. Lee KY, Ryu SH, Suh PG, Choi WC, Rhee SG (1987): Phospholipase C associated with particulate fractions of bovine brain. Proc Natl Acad Sci USA 84:5540–5544PubMedGoogle Scholar
  75. Leimeister-Wächter M, Domann E, Chakraborty T (1991): Detection of a gene-encoding Pi-specific phospholipase C that is coordinately expressed with listeriolysin in Listeria monocytogenes. Mol Microbiol 5:361–366PubMedGoogle Scholar
  76. Levine L, Xiao DM, Little C (1987): Increased arachidonic acid metabolites from cells in culture after treatment with phospholi-pase C from Bacillus cereus. Prostaglandins 34:633–642PubMedGoogle Scholar
  77. Lewis K, Garigapati V, Zhou C, Roberts MF (1993). Substrate requirements of bacterial phosphatidylinositol-specific phospholipase C. Biochemistry 32:8836–8841PubMedGoogle Scholar
  78. Liemann S, Lewit-Bentley A (1995): Annexins: a novel family of calcium- and membrane-binding proteins in search of a function. Structure 3:233–237PubMedGoogle Scholar
  79. Little C (1981): Effect of some divalent metal cations on phospholipase C from Bacillus cereus. Acta Chem Scand B35:39–44Google Scholar
  80. Little C, Johansen S (1979): Unfolding and refolding of phospholipase C in solutions of guanidium chloride. Biochem J 179:509–514PubMedGoogle Scholar
  81. Low, MG (1981): Phosphatidylinositol-specific phospholipase C from Bacillus thuringiensis. Meth Enzymol 71:741–746PubMedGoogle Scholar
  82. Majerus PW (1992): Inositol phosphate biochemistry. Annu Rev Biochem 61:225–250PubMedGoogle Scholar
  83. Martin SF, Wong Y-L, Wagman AS (1994): Design, synthesis and evolution of phospholipid analogues as inhibitors of the bacterial phospholipase C from Bacillus cereus. J Org Chem 59:4821–4831Google Scholar
  84. Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C (1992): Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356:615–618PubMedGoogle Scholar
  85. Martinez C, Nicolas A, van Tilbeurgh H, Egloff M-P, Cudrey C, Verger R, Cambillau C (1994): Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry 33:83–89PubMedGoogle Scholar
  86. Meers P, Mealy T (1994): Phospholipid determinants for annexin V binding sites and the role of tryptophan 187. Biochemistry 33:5829–5837PubMedGoogle Scholar
  87. Meers P, Mealy T (1993): Relationship between annexin V tryptophan exposure, calcium, and phospholipid binding. Biochemistry 32:5411–5418PubMedGoogle Scholar
  88. Mengaud J, Braun-Breton C, Cossart P (1991): Identification of phosphatidylinositol-specific phospholipase C activity in Listeria monocytogenes: A novel type of virulence factor? Mol Microbiol 5:367–372PubMedGoogle Scholar
  89. Moolenaar WH (1994): LPA: a novel lipid mediator with diverse biological actions. Trends Cell Biol 4:213–219PubMedGoogle Scholar
  90. Moss SE, ed. (1992): The Annexins. London: PortlandGoogle Scholar
  91. Mosser G, Ravanat C, Freyssinet J-M, Brisson A (1991): Sub-domain structure of lipid-bound annexin-V resolved by electron image analysis. J Mol Biol 217:241–245PubMedGoogle Scholar
  92. Murayama T, Ui M (1987): Phosphatidic acid may stimulate membrane receptors mediating adenylate cyclase inhibition and phospholipid breakdown in 3T3 fibroblasts.J Biol Chem 262:5522–5529PubMedGoogle Scholar
  93. Newman R, Tucker AD, Ferguson C, Tsernoglou D, Leonard K, Crumpton MJ (1989): Crystallization of p68 on lipid monolayers and as three-dimensional crystals.J Mol Biol 206:213–219PubMedGoogle Scholar
  94. Noble MEM, Cleasby A, Johnson LN, Egmond MR, Frenken LGJ (1993): The crystal structure of a triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett 331:123–128PubMedGoogle Scholar
  95. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Sussman JL, Verschueren KHG, Goldman A (1992): The α/β hydrolase fold. Prot Engin 5:197–211Google Scholar
  96. Pelech SL, Vance DE (1989): Signal transduction via phosphatidylcholine cycles. Trends Biochem Sci 14:28–30Google Scholar
  97. Pepinsky RB, Tizard R, Mattaliano RJ, Sinclair LK, Miller GT, Browning JL, Chow EP, Burne C, Huang K-S, Pratt D, Wächter L, Hession C, Frey AZ, Wallner BP (1988): Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. J Biol Chem 263:10799–10811PubMedGoogle Scholar
  98. Pieterson JC, Vidal JC, Volwerk JJ, DeHaas GH (1974): Zymogen-catalyzed hydrolysis of monomeric substrates and the presence of a recognition site for lipid-water interfaces in phospholipase A2. Biochemistry 13:1455–1460PubMedGoogle Scholar
  99. Pigault C, Follenius-Wund A, Schmutz M, Freyssinet J-M, Brisson A (1994): Formation of two-dimensional arrays of annexin V on phosphatidylserine-containing liposomes. J Mol Biol 236:199–208PubMedGoogle Scholar
  100. Pollard HB, Guy HR, Arispe N, de la Fuente M, Lee G, Rojas EM, Pollard JR, Srivastava M, Zhang-Keck Z-Y, Merezhinskaya N, Caohuy H, Burns AL, Rojas E (1992): Calcium channel and membrane fusion activity of synexin and other members of the annexin gene family. Biophys J 62:15–18PubMedGoogle Scholar
  101. Raynal P, Pollard, HB (1994): Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biophys Biochim Acta 1197:63–93Google Scholar
  102. Renetseder R, Dijkstra BW, Huizing K, Kalk KH, Drenth J (1988): Crystal structure of bovine pancreatic phospholipase A2 covalently inhibited by p-bromo-phenacyl-bromide.J Mol Biol 200:181–188PubMedGoogle Scholar
  103. Reynolds LJ, Hughes LL, Louis AI, Kramer RM, Dennis EA (1993): Metal ion and salt effects on the phospholipase A2, lysophospholipase, and transacylase activities of human cytosolic phospholipase A2. Biochim Biophys Acta 1167:272–280PubMedGoogle Scholar
  104. Rhee SG, Choi KD (1992a): Regulation of inositol phospholipid-specific phospholipase C isozymes.J Biol Chem 267:12393–12396PubMedGoogle Scholar
  105. Rhee SG, Choi KD (1992b): Multiple forms of phospholipase C isozymes and their activation mechanisms. Adv Second Messenger Phosphoprot Res 26:35–61Google Scholar
  106. Rhee SG, Suh PG, Ryu S-H, Lee KY (1989): Studies of inositol phospholipid-specific phospholipase C. Science 244:546–550PubMedGoogle Scholar
  107. Roberts MF (1991): Using short-chain phospholipids to assay phospholipases. Meth Enzymol 197:95–112PubMedGoogle Scholar
  108. Roberts MF, Dennis EA (1989): The role of phospholipases in phosphatidylcholine catabolism. In: Phosphatidylcholine Metabolism, Vance DE, ed. New York: CRC PressGoogle Scholar
  109. Roholt O, Schlamowitz M (1961): L-α-(dicaproyl)lecithin, a soluble substrate for lecithinase A and D. Arch Biochem Biophys 94:364–379PubMedGoogle Scholar
  110. Russo-Marie F (1992): Annexins, phospholipase A2 and the glucocorticoids. In: The Annexins, Moss S, ed. New York: Portland PressGoogle Scholar
  111. Salmon DM, Honeyman TW (1980): Proposed mechanism of cholinergic action in smooth muscle. Nature 284:344–345PubMedGoogle Scholar
  112. Schrag JD, Li Y, Wu S, Cygler M (1991): Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature 351:761–764PubMedGoogle Scholar
  113. Scott D, White SP, Browning JL, Rosa JJ, Gelb MH, Sigler PB (1991): Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. Science 254:1007–1010PubMedGoogle Scholar
  114. Scott D, White SP, Otwinowski Z, Yuan W, Gelb M, Sigler PB (1990): Interfacial catalysis: the mechanism of phospholipase A2. Science 250:1541–1546PubMedGoogle Scholar
  115. Seaton BA, ed. (1996): Annexins: Molecular Structure to Cellular Function, Austin, TX: R G Landes CompanyGoogle Scholar
  116. Sharp JD, Pickard RT, Chiou XG, Manetta JV, Kovacevic S, Miller JR, Roberts EF, Strifler BA, Brems DN, Kramer RM (1994): Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2.J Biol Chem 269:23250–23254PubMedGoogle Scholar
  117. Soltys CE, Bian J, Roberts, MF (1993): Polymerizable phosphatidylcholines: Importance of phospholipid motions for optimum phospholipase A2 and C activity. Biochemistry 32:9545–9552PubMedGoogle Scholar
  118. Sopkova J, Renouard M, Lewit-Bentley A (1993): The crystal structure of a new high-calcium form of annexin V.J Mol Biol 234:816–825PubMedGoogle Scholar
  119. Soriano-Garcia M, Padmanabhan K, de Vos A, Tulinsky A (1992): The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1. Biochemistry 31:2554–2566PubMedGoogle Scholar
  120. Sundell S, Hansen S, Hough E (1994): A proposal for the catalytic mechanism in phospholipase C based on interaction energy and distance geometry calculations. Prot Engin 7:571–577Google Scholar
  121. Sunnerhagen M, Forsén S, Hoffren A-M, Drakenberg T, Teleman O, Stenflo J (1995): Structure of the Ca2+-free Gla domain sheds light on membrane binding of blood coagulation proteins. Nature Struct Biol 2:968–974Google Scholar
  122. Swairjo MA, Seaton BA (1995): unpublished dataGoogle Scholar
  123. Swairjo MA, Seaton BA (1994): Annexin structure and membrane interactions: a molecular perspective. Ann Rev Biophys Biomol Struct 23:193–213Google Scholar
  124. Swairjo MA, Concha NO, Kaetzel MA, Dedman JR, Seaton BA (1995): Ca2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nature Struct Biol 2:968–974PubMedGoogle Scholar
  125. Swairjo MA, Roberts MF, Campos M-B, Dedman JR, Seaton BA (1994): Annexin V binding to the outer leaflet of small unilamellar vesicles leads to altered inner-leaflet properties: 31P- and 1H-NMR studies. Biochemistry 33:10944–10950PubMedGoogle Scholar
  126. Taguchi R, Ikezawa H (1978): PI-specific PLC from colestium. Arch Biochem Biophys 186:196–201PubMedGoogle Scholar
  127. Tait JF, Gibson D, Fujikawa K (1989): Phospholipid binding properties of human placental anticoagulant protein-I, a member of the lipocortin family.J Biol Chem 264:7944–7949PubMedGoogle Scholar
  128. Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M (1995): Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium free state. Nature 376:444–447PubMedGoogle Scholar
  129. Thunnissen MMGM, Kalk KH, Drenth J, Dijkstra BW (1990): Structure of an engineered porcine phospholipase A2 with enhanced activity at 2.1 Á resolution. J Mol Biol 216:425–439PubMedGoogle Scholar
  130. Uppenberg J, Hansen MT, Patkar S, Jones TA (1994): The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure 2:293–308PubMedGoogle Scholar
  131. Van Blitterswijk, Hilkmann H (1993): Rapid attenuation of receptor-induced diacylglycerol and phosphatidic acid by phospholipase D-mediated transphosphorylation: Formation of bisphosphatidic acid. EMBO J 12:2655–2662PubMedGoogle Scholar
  132. van Tilbeurgh H, Egloff M-P, Martinez C, Rugani N, Verger R, Cambillau C (1993): Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature 362:814–820PubMedGoogle Scholar
  133. van Tilbeurgh H, Roussel A, Lalouel J-M, Cambillau C (1994): Lipoprotein lipase. Molecular model based on the pancreatic lipase X-ray structure: Consequences for heparin binding and catalysis. J Biol Chem 269:4626–4633PubMedGoogle Scholar
  134. van Tilbeurgh H, Sarda L, Verger R, Cambillau C (1992): Structure of the pancreatic lipase-procolipase complex. Nature 359:159–162PubMedGoogle Scholar
  135. Vega QC, Cochet C, Filhol O, Chang CP Rhee SG, Gill GN (1992): A site of tyrosine phosphorylation in the C terminus of the epidermal growth factor receptor is required to activate phospholipase C. Mol Cell Biol 12:128–135PubMedGoogle Scholar
  136. Verheij HM, Slotboom AJ, De Haas GH (1981): Phospholipase A2: a model for membrane-bound enzymes. Rev Physiol Pharmacol 91:91–203Google Scholar
  137. Voges D, Berendes R, Burger A, Demange P, Baumeister W, Huber H (1994): Three-dimensional structure of membrane-bound annexin V, a correlative electron microscopy X-ray crystallography study.J Mol Biol 238:199–213PubMedGoogle Scholar
  138. Volwerk JJ, Shashidhar MS, Kuppe A (1990): Pi-specific PLC from Bacillus cereus combines intrinsic phosphotransferase and cyclic phosphodiesterase activities: A 31-NMR study. Biochemistry 29:8056–8062PubMedGoogle Scholar
  139. Wery J-P, Schevitz RW, Clawson DK, Bobbitt JL, Dow ER, Gamboa G, Goodson T, Hermann RB, Kramer RM, McClure DB, Mihelich ED, Putnam JE, Sharp JD, Stark DH, Teater C, Warrick MW, Jones ND (1991): Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 Å resolution. Nature 352:79–82PubMedGoogle Scholar
  140. Wells MA (1974): The mechanism of interfacial activation of phospholipase A2. Biochemistry 13:2248–2257PubMedGoogle Scholar
  141. Weng X, Luecke H, Song IS, Kang DS, Kim S-H, Huber R (1993): Crystal structure of human annexin I at 2.5 Å resolution. Protein Science 2:448–458PubMedGoogle Scholar
  142. White SP, Scott DL, Otwinowski Z, Gelb MH, Sigler PB (1990): Crystal structure of cobra venom phospholipase A2 in a complex with a transition state analogue. Science 250:1560–1563PubMedGoogle Scholar
  143. Winkler FK, D-Arcy A, Hunziker W (1990): Structure of human pancreatic lipase. Nature 343:771–774PubMedGoogle Scholar

Copyright information

© Birkhäuser Boston 1996

Authors and Affiliations

  • Barbara A. Seaton
  • Mary F. Roberts

There are no affiliations available

Personalised recommendations