Skip to main content

The Three Dimensional Structure of SAP

  • Chapter
  • 57 Accesses

Part of the book series: Argenteuil Symposia ((ARGENTEUIL))

Abstract

Serum amyloid P (SAP) component and C-reactive protein (CRP) are members of a closely related family of pentameric or decameric proteins called pentraxins which are involved in amyloidosis and the acute phase response (Pepys and Baltz 1983). Although CRP was crystallised in 1947 (McCarty 1947), no detailed three dimensional structural information has been obtained by X-ray analysis. However, several recent reports of CRP (DeLucas et al. 1987) and SAP (Wood et al. 1988) crystals have demonstrated that this is now a realistic objective. In this paper we review progress made on the X-ray analysis in our laboratory, and describe for the first time preliminary, medium resolution electron density maps of a pentameric form of SAP.

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Anderson JK, Taylor JA, Baltz ML et al. (1989) Primary structure of murine serum amyloid P component (submitted)

    Google Scholar 

  • Baltz ML, de Beer FC, Feinstein A et al. (1982a) Phylogenetic aspects of C-reactive protein and related proteins. Ann NY Acad Sci 389: 49–75

    Article  PubMed  CAS  Google Scholar 

  • Baltz ML, de Beer FC, Feinstein A, Pepys MB (1982b) Calcium-dependent aggregation of human serum amyloid P component. Biochim Biophys Acta 701: 229–236

    Article  PubMed  CAS  Google Scholar 

  • Bricogne G (1976) Methods and programs for direct-space exploitation of geometric redundancies. Acta Cryst A32: 832–847

    Google Scholar 

  • Crowther RA (1972) In: Rossman MG (ed) The molecular replacement method. Gordon and Breach, pp 173–175

    Google Scholar 

  • DeLucas LJ, Greenhough TJ, Rule SA (1987) Preliminary X-ray study of crystals of human C-reactive protein. J Mol Biol 196: 741–742

    Article  PubMed  CAS  Google Scholar 

  • Hawkins PN, Myers MJ, Lavender JP, Pepys MB (1988) Diagnostic radionuclide imaging of amyloid: biological targeting by circulating human serum amyloid P component. Lancet i: 1413–1418

    Google Scholar 

  • Hind CRK, Collins PM, Renn D et al. (1984a) Binding specificity of serum amyloid P-component for the pyruvate acetal of galactose. J Exp Med 159: 1058–1069

    Article  PubMed  CAS  Google Scholar 

  • Hind CRK, Collins PM, Pepys MB (1984b) Calcium-dependent aggregation of human serum amyloid P component. Inhibition of the cyclic 4,6-pyruvate acetal of galactose. Biochim Biophys Acta 802: 148–150

    Article  PubMed  CAS  Google Scholar 

  • McCarty MJ (1947) The occurrence during acute infections of a protein not normally present in the blood IV. Crystallization of the C-reactive protein. J Exp Med 85: 491–498

    Article  PubMed  CAS  Google Scholar 

  • McCarty MJ (1982) Historical perspective on C-reactive protein. Ann NY Acad Sci 389: 1–9

    Article  PubMed  CAS  Google Scholar 

  • Ngkuyen NY, Suzuki A, Boykins RA, Liu T-Y (1986) The amino acid sequence of Limulus C-reactive protein. Evidence of polymorphism. J Biol Chem 261: 10456–10465

    Google Scholar 

  • O’Hara BP, Wood SP, Oliva G et al. (1988) Crystallizations of human serum amyloid P component (SAP). J Crystal Growth 90: 209–212

    Article  Google Scholar 

  • Oliva G, O’Hara BP, Wood SP et al. (1986) Preliminary crystallographic studies of human serum amyloid P component (SAP). In: Peeters H (ed) Protides of the biological fluids, vol 34. Pergamon Press, Oxford, pp 371–374

    Google Scholar 

  • Osmand AP, Freidenson B, Gewurz H (1977) The characteristics of C-reactive protein and the complement subcomponent Clt as homologous proteins displaying cyclic pentameric symmetry (pentraxins). Proc Natl Acad Sci USA 74: 739–743

    Article  PubMed  CAS  Google Scholar 

  • Painter RH, Pintenc L, Hoffman T, Kells DIC, Katz A (1976) Ultrastructure and chemistry of Clt subcomponent of CI: Similarities to amyloid P-component. J Immunol 116: 1745

    Google Scholar 

  • Painter RH, de Escallion I, Massey A et al. (1982) The structure and binding characteristics of serum amyloid protein (9.5S α1-glycoprotein). Ann NY Acad Sci 389: 199–215

    Article  PubMed  CAS  Google Scholar 

  • Pepys MB, Baltz ML (1983) Acute phase proteins with special reference to C-reactive protein and related proteins and serum amyloid A protein. Adv Immunol 34: 141–212

    Article  PubMed  CAS  Google Scholar 

  • Pepys MB, Butler PJG (1987) Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum. Biochem Biophys Res Commun 148: 308–313

    Article  PubMed  CAS  Google Scholar 

  • Pepys MB, Dash AC, Munn EA, Feinstein A, Skinner M, Cohen AS, Gewurz H, Osmand AP, Painter RH (1977) Isolation of amyloid P-component (protein AP) from normal serum as a calcium-dependent binding protein. Lancet i: 1029–1031

    Google Scholar 

  • Perkins SJ, Pepys MB (1986) X-ray and neutron scattering studies on CRP and SAP. In: Peeters H (ed) Protides of the biological fluids colloquium XXXIV. Pergamon Press, Oxford, pp 323–326

    Google Scholar 

  • Taylor WR (1986a) The classification of amino acid conservation. J Theor Biol 119: 205–218

    Article  PubMed  CAS  Google Scholar 

  • Taylor WR (1986b) Identification of protein sequence homology by consensus template alignment. J Mol Biol 188: 233–258

    Article  PubMed  CAS  Google Scholar 

  • Turnell WG (1989) Searches for calcium-binding motifs in protein sequences. In: Reid E, Cook GMW, Luzio JP (eds) Biochemical approaches to cellular calcium. Royal Soc Chem, London (Methodological surveys in biochemistry and analysis, vol 19) (in press)

    Google Scholar 

  • Turnell WG, Satchwell SC, Travers AA (1988) Hypothesis: a decapeptide motif for binding to the minor groove of DNA—a proposal. FEBS Lett 232: 263–268

    Article  PubMed  CAS  Google Scholar 

  • Wang BC (1985) Resolution of phase ambiguity in macromolecular crystallography. Meth Enzymol 115: 90–112

    Article  PubMed  CAS  Google Scholar 

  • Wood SP, Blundell TL, Wollmer A et al. (1975) The relation of conformation and association of insulin to receptor binding; X-ray and circular dichroism studies on bovine and hystriomorph insulins. Eur J Biochem 55: 531–542

    Article  PubMed  CAS  Google Scholar 

  • Wood SP, Oliva G, O’Hara BP et al. (1988) A pentameric form of human serum amyloid P component. Crystallization, X-ray diffraction and neutron scattering studies. J Mol Biol 202: 169–173

    Article  PubMed  CAS  Google Scholar 

  • Young NM, Williams RE (1978) Comparison of the secondary structures and binding of C-reactive protein and the phosphorylcholine-binding murine myeloma proteins. J Immunol 121: 1893–1898

    PubMed  CAS  Google Scholar 

Download references

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1989 Springer-Verlag London Limited

About this chapter

Cite this chapter

White, H.E., O’Hara, B.P., Oliva, G., Blundell, T.L., Pepys, M.B., Wood, S.P. (1989). The Three Dimensional Structure of SAP. In: Pepys, M.B. (eds) Acute Phase Proteins in the Acute Phase Response. Argenteuil Symposia. Springer, London. https://doi.org/10.1007/978-1-4471-1739-1_10

Download citation

  • DOI: https://doi.org/10.1007/978-1-4471-1739-1_10

  • Publisher Name: Springer, London

  • Print ISBN: 978-1-4471-1741-4

  • Online ISBN: 978-1-4471-1739-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics