2a55
From Proteopedia
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Solution structure of the two N-terminal CCP modules of C4b-binding protein (C4BP) alpha-chain.
Overview
Human C4b-binding protein (C4BP) protects host tissue, and those pathogens, able to hijack this plasma glycoprotein, from complement-mediated, destruction. We now show that the first two complement control protein, (CCP) modules of the C4BP alpha-chain, plus the four residues connecting, them, are necessary and sufficient for binding a bacterial virulence, factor, the Streptococcus pyogenes M4 (Arp4) protein. Structure, determination by NMR reveals two tightly coupled CCP modules in an, elongated arrangement within this region of C4BP. Chemical shift, perturbation studies demonstrate that the N-terminal, hypervariable region, of M4 binds to a site including strand 1 of CCP module 2. This interaction, is accompanied by an intermodular reorientation within C4BP. We thus, provide a detailed picture of an interaction whereby a pathogen evades, complement.
About this Structure
2A55 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor., Jenkins HT, Mark L, Ball G, Persson J, Lindahl G, Uhrin D, Blom AM, Barlow PN, J Biol Chem. 2006 Feb 10;281(6):3690-7. Epub 2005 Dec 5. PMID:16330538
Page seeded by OCA on Mon Nov 12 20:46:23 2007
Categories: Homo sapiens | Single protein | Ball, G. | Barlow, P.N. | Blom, A.M. | Jenkins, H.T. | Lindahl, G. | Mark, L. | Uhrin, D. | Ccp module | Complement | Scr
