1gkn
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(New page: 200px<br /> <applet load="1gkn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gkn" /> '''STRUCTURE DETERMINATION AND RATIONAL MUTAGE...)
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Revision as of 15:00, 12 November 2007
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STRUCTURE DETERMINATION AND RATIONAL MUTAGENESIS REVEAL BINDING SURFACE OF IMMUNE ADHERENCE RECEPTOR, CR1 (CD35)
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Blood group, Knops system OMIM:[120620], CR1 deficiency OMIM:[120620], Malaria, severe, resistance to OMIM:[120620], SLE susceptibility OMIM:[120620]
About this Structure
1GKN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 17:06:45 2007
Categories: Homo sapiens | Single protein | Atkinson, J.P. | Barlow, P.N. | Bromek, K. | Hauhart, R.E. | Krych-Goldberg, M. | Mallin, R.L. | Smith, B.O. | Uhrin, D. | Wang, X. | Complement | Module | Scr | Structure