1lim

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

COMPARATIVE ANALYSES OF PENTRAXINS: IMPLICATIONS FOR PROTOMER ASSEMBLY AND LIGAND BINDINGCOMPARATIVE ANALYSES OF PENTRAXINS: IMPLICATIONS FOR PROTOMER ASSEMBLY AND LIGAND BINDING

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed 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 beta-jelly roll topology and a hydrophobic core similar to that seen in SAP. Only minor differences are observed in the positions of residues involved in coordinating calcium ions. CONCLUSIONS: 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. Comparative analyses of pentraxins: implications for protomer assembly and ligand binding.,Srinivasan N, White HE, Emsley J, Wood SP, Pepys MB, Blundell TL Structure. 1994 Nov 15;2(11):1017-27. PMID:7881902 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1lim Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image