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 Thu Feb 21 16:23:42 2008
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
