1gop

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

STRUCTURE OF THE C3B-BINDING SITE OF CR1 (CD35), THE IMMUNE ADHERENCE RECEPTOR

spinqualitylabelsall models 1gop Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Complement receptor type 1 (CR1 or CD35) is a multiple modular protein that mediates the immune adherence phenomenon, a fundamental event for destroying microbes and initiating an immunological response. It fulfills this role through binding C3b/C4b-opsonized foreign antigens. The structure of the principal C3b/C4b binding site (residues 901-1095) of CR1 is reported, revealing three complement control protein modules (modules 15-17) in an extended head-to-tail arrangement with flexibility at the 16-17 junction. Structure-guided mutagenesis identified a positively charged surface region on module 15 that is critical for C4b binding. This patch, together with basic side chains of module 16 exposed on the same face of CR1, is required for C3b binding. These studies reveal the initial structural details of one of the first receptor-ligand interactions to be identified in immunobiology. Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor.,Smith BO, Mallin RL, Krych-Goldberg M, Wang X, Hauhart RE, Bromek K, Uhrin D, Atkinson JP, Barlow PN Cell. 2002 Mar 22;108(6):769-80. PMID:11955431 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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