Comparative analyses of pentraxins: implications for protomer assembly and ligand binding

N. Srinivasan, Helen E. White, Jonas Emsley, Steve P. Wood, Mark B. Pepys, Tom L. Blundell

Research output: Contribution to journalArticlepeer-review


Background: Pentraxins are a family of plasma proteins characterized by their pentameric assembly and calcium–dependent ligand binding. The recent determination of the crystal structure for a member of this family, human serum amyloid P component (SAP), provides a basis for the comparative analysis of the pentraxin family.

Results: We have compared the sequences, tertiary structures and quaternary arrangements of SAP with human C–reactive protein (CRP), Syrian hamster SAP (HSAP) and Limulus polyphemus CRP (LIM). These proteins can adopt a β–jelly roll topology and a hydrophobic core similar to that seen in SAP. Only minor differences are observed in the positions of residues Sinvolved in coordinating calcium ions.

Calcium–mediated ligand binding by CRP, HSAP and LIM is similar to that defined by the crystal structure of SAP, but sequence differences in the hydrophobic pocket explain the differential ligand specificities exhibited by the homologous proteins. Differences elsewhere, including insertions and deletions, account for the different (hexameric) quaternary structure of LIM.
Original languageEnglish
Pages (from-to)1017-1027
Issue number11
Publication statusPublished - 1 Nov 1994


Dive into the research topics of 'Comparative analyses of pentraxins: implications for protomer assembly and ligand binding'. Together they form a unique fingerprint.

Cite this