2nyz
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(New page: 200px<br /><applet load="2nyz" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nyz, resolution 2.60Å" /> '''Viral Chemokine Bind...)
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Revision as of 09:25, 23 January 2008
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Viral Chemokine Binding Protein M3 From Murine Gammaherpesvirus68 In Complex With The C- Chemokine XCL1
Overview
Viruses have evolved a myriad of evasion strategies focused on undermining, chemokine-mediated immune surveillance, exemplified by the mouse, gamma-herpesvirus 68 M3 decoy receptor. Crystal structures of M3 in, complex with C chemokine ligand 1/lymphotactin and CC chemokine ligand, 2/monocyte chemoattractant protein 1 reveal that invariant chemokine, features associated with G protein-coupled receptor binding are primarily, recognized by the decoy C-terminal domain, whereas the N-terminal domain, (NTD) reconfigures to engage divergent basic residue clusters on the, surface of chemokines. Favorable electrostatic forces dramatically enhance, the association kinetics of chemokine binding by M3, with a primary role, ascribed to acidic NTD regions that effectively mimic glycosaminoglycan, interactions. Thus, M3 employs two distinct mechanisms of chemical, imitation to potently sequester chemokines, thereby inhibiting chemokine, receptor binding events as well as the formation of chemotactic gradients, necessary for directed leukocyte trafficking.
About this Structure
2NYZ is a Protein complex structure of sequences from Murid herpesvirus 2. Full crystallographic information is available from OCA.
Reference
Dual GPCR and GAG mimicry by the M3 chemokine decoy receptor., Alexander-Brett JM, Fremont DH, J Exp Med. 2007 Dec 24;204(13):3157-72. Epub 2007 Dec 10. PMID:18070938
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