Abstract
Human brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and 15N-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the 1H and 15N resonances were achieved by applying multidimensional homo- and heteronuclear NMR experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a total of 2490 meaningful distance constraints. The overall B-FABP structure exhibits the typical backbone conformation described for other members of the FABP family, consisting of ten antiparallel β-strands (βA to βJ) that form two almost orthogonal β-sheets, a helix-turn-helix motif that closes the β-barrel on one side, and a short N-terminal helical loop. A comparison with the crystal structure of the same protein complexed with docosahexaenoic acid [12] reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity. (Mol Cell Biochem 239: 61–68, 2002)
Key words
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
Abbreviations
- 2D:
-
two-dimensional
- 3D:
-
three-dimensional
- CRBP:
-
cellular retinol-binding protein
- CRABP:
-
cellular retinoic acid-binding protein
- DHA:
-
docosahexaenoic acid
- FA:
-
fatty acid
- FABP:
-
fatty acid-binding protein
- A-FABP:
-
adipocyte-type FABP
- B-FABP:
-
brain-type FABP
- H-FABP:
-
heart-type FABP
- I-FABP:
-
intestinal-type FABP
- ILBP:
-
ileal lipid-binding protein
- L-FABP:
-
liver-type FABP
- M-FABP:
-
myelin-type FABP
- HSQC:
-
heteronuclear single-quantum correlation
- NOE:
-
nuclear Overhauser effect
- NOESY:
-
nuclear Overhauser enhancement and exchange spectroscopy
- TOCSY:
-
total correlation spectroscopy
- RMSD:
-
root-mean-square deviation
References
Vcerkamp JH, Maatman RGHJ: Cyloplasmic fatly acid-binding proteins: Their structure and genes. Prog Lipid Res 34: 17–52, 1995
Hohoff C, Spencr F: Fatty acid binding proteins and mammary-derived growth inhibitor. Fett Lipid 100: 252–263, 1998
Veerkamp JH, Zimmerman AW: Fatty acid-binding proteins of nervous tissue. J Mol Neurosci 16: 133–142, 2001
Owada Y, Yoshimoto T, Kondo H: Spatio-temporally differential expression of genes for three members of fatty acid binding proteins in developing and mature rat brains. J Chem Neuroanat 12: 113–122, 1996
Feng L, Hatten ME, Heintz N: Brain lipid-binding protein (BLBP): A novel signaling system in the developing mammalian CNS, Neuron 12: 895–908, 1994
Kurtz A, Zimmer A, Schnütgen F. Briining G, Spener F. Müller T: The expression pattern of a novel gene encoding brain fatty-acid binding protein correlates with neuronal and glial cell development. Development 120: 2637–2649, 1994
Godbout R, Bisgrove DA, Shkolny D. Day RS: Correlation of B-FABP and GFAP expression in malignant glioma. Oneogene 16: 1955–1963, 1998
Xu LZ, Sánchez R. Sali A, Heintz N: Ligand specificity of brain lipid-binding protein. J Biol Chem 271: 24711–24719, 1996
Richieri GV, Ogata RT, Zimmerman AW, Veerkamp JH, Kleinfeld AM: Fatty acid binding proteins from different tissues show distinct patterns of fatty acid interactions. Biochemistry 39: 7197–7204, 2000
Zimmerman AW, van Moerkerk HTB, Veerkamp JH: Ligand specificity and conformational stability of human fatty acid-binding proteins. Int J Bioehcm Cell Biol 33: 865–876, 2001
Green P, Glozman S, Kamensky B, Yavin E: Developmental changes in rat brain membrane lipids and fatty acids: The preferential prenatal accumulation of docosahexaenoic acid. J Lipid Res 40: 960–966, 1999
Balendiran GK, Schniitgen F, Scapin G, Börchers T, Xhong N, Lim K, Godbout R, Spener F, Sacchettini JC: Crystal structure and thermodynamie analysis of human brain fatty acid-binding protein. J Biol Chem 275: 27045–27054, 2000
Zimmerman AW, Rademachcr M, Riitcrjans H, Lücke C, Veerkamp JH: Functional and conformational characterization of new mutants of heart fatty acid-binding protein. Biochem J 344: 495–501, 1999
Kay LE, Keifer P, Saarinen T: Pure absorption gradient enhanced heteronuclear single quantum correlation speetroscopy with improved sensitivity. J Am Chem Soc 114: 10663–10665, 1992
Schleueher J, Sattler M, Griesinger C: Coherence selection via gradients without loss of sensitivity. The 3D-HNCO experiment. Angew Chem Int Ed Eng 32: 1489–1491, 1993
Wishart DS, Bigam CG, Yao J. Abildgaard F, Dyson HJ, Oldfield E, Marklcy JL, Sykes BD: 1H.13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6: 135–140, 1995
Wüthrich K: NMR of Proteins and Nucleic Acids. Wiley, New York, 1986
Pristovsek P, Lücke C. Reinckc B. Ludwig B, Rüterjans H: Solution structure of the functional domain of Paracoccus denitrificans cytochrome c 552 in the reduced state. Fur J Biochem 267: 4205–4212. 2000
Güntert P. Mumenthaler C. Wüthrich K: Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273: 283–298, 1997
Giintert P, Braun W, Wüthrich K: Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA, J Mol Biol 217: 517–530, 1991
Wüthrich K, Billeter M. Braun W: Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton—proton distance constraints with nuclear magnetic resonance. J Mol Biol 169: 949–961, 1983
Dauber-Osguthorpe P, Roberts VA, Osguthorpe DJ, Wolff DJ, Genest M, Hagler AT: Structure and energetics of ligand binding to proteins: E. coli dihydrofolate reductasc trimethoprin, a drugreceptor system. Proteins 4: 31–47, 1988
Laskowski RA, MacArthur MW, Moss DS, Thornton JM: AQUA and PROCHFCK-NMR: Programs for checking the quality of protein structures solved by NMR. J Appl Crystallogr 26: 283–291, 1993
Noy N: Retinoid-binding proteins: Mediators of retinoid action. Biochem J 348: 481–495, 2000
Folli C, Calderone V, Ottoncllo S, Bolchi A, Zanotti G, Stoppini M, Rudolfo B: Identification, retinoid binding, and X-ray analysis of a human retinol-binding protein. Proc Natl Acad Sci USA 98: 3710–3715, 2001
Lücke C, Pérez C, Cavazzini D, Rademacher M, Ludwig C, Spisni A, Rossi GL, Rüterjans H: Structure and backbone dynamics of apo-and holo-cellular retinol-binding protein in solution. J Biol Chem 277: 21983–21997, 2002
Gutiérrez-Gonzalez LH, Ludwig C, Hohoff C, Rademacher M, Hanhoff T, Rüterjans H, Spener F, Lücke C: Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP). Biochem J 364: 725–737, 2002
Hodsdon ME, Cistola DP: Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: Implications for the mechanism of ligand entry. Biochemistry 36: 1450–1460, 1997
Zhang F. Lücke C, Baicr LJ, Sacchettini JC, Hamilton JA: Solution structure of human intestinal fatty acid-binding protein: Implications for ligand entry and exit. J Biomol NMR 9: 213–228, 1997
Lücke C, Zhang F, Rüterjans H, Hamilton JH, Sacchettini JC: Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein. Structure 4: 785–800, 1996
Lu J. Lin C-L, Tang C. Ponder JW, Kao JLF, Cistola DP, Li F: The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: Comparison with the X-ray structure. J Mol Biol 286: 1179–1195, 1999
Wang L, Li Y, Abildgaard F, Markley JL, Yan H: NMR solution structure of type II human cellular retinoic acid binding protein: Implications for ligand binding. Biochemistry 37: 12727–12736, 1998
Constantine KL, Friedrichs MS, Wittekind M, Jamil H, Chu C-H, Parker RA, Goldfarb V, Mueller L. Farmer BT: Backbone and side chain dynamics of uneomplexed human adipoeyte and muscle fatty acid-binding proteins. Biochemistry 37: 7965–7980, 1998
Lassen D. Lücke C, Kveder M, Mesgarzadeh A, Schmidt JM, Specht B. Lezius A, Spener F, Rüterjans H: Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy. Eur J Biochem 230: 266–280, 1995
Lücke C, Rademachcr M, Zimmerman AW, van Moerkerk HTB, Veerkamp JH, Rüterjans H: Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP). Biochem J 354: 259–266, 2001
Wishart DS, Sykes BD, Richards FM: Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222: 311–333, 1991
Lücke C, Huang S, Rademacher M, Rüterjans H: New insights into intracellular lipid binding proteins: The role of buried water. Prot Sci (in press)
Young ACM, Seapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC: Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: Binding interactions with three C18 fatty acids. Structure 2: 523–534, 1994
Kraulis PJ: MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24: 946–950, 1991
Merritt EA, Bacon DJ: Raster3D: Photorealistic molecular graphics. Meth Enzymol 277: 505–524, 1997
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Rademacher, M., Zimmerman, A.W., Rüterjans, H., Veerkamp, J.H., Lücke, C. (2002). Solution structure of fatty acid-binding protein from human brain. In: Glatz, J.F.C. (eds) Cellular Lipid Binding Proteins. Developments in Molecular and Cellular Biochemistry, vol 38. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9270-3_8
Download citation
DOI: https://doi.org/10.1007/978-1-4419-9270-3_8
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-4868-9
Online ISBN: 978-1-4419-9270-3
eBook Packages: Springer Book Archive