2ffk
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(New page: 200px<br /> <applet load="2ffk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ffk" /> '''Solution structure of the complex between p...)
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Revision as of 19:58, 12 November 2007
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Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta, minimized average structure
Overview
Chemokines (chemotactic cytokines) comprise a large family of proteins, that recruit and activate leukocytes, giving chemokines a major role in, both immune response and inflammation-related diseases. The, poxvirus-encoded viral CC chemokine inhibitor (vCCI) binds to many CC, chemokines with high affinity, acting as a potent inhibitor of chemokine, action. We have used heteronuclear multidimensional NMR to determine the, structure of an orthopoxvirus vCCI in complex with a human CC chemokine, MIP-1beta (macrophage inflammatory protein 1beta). vCCI binds to the, chemokine with 1:1 stoichiometry, forming a complex of 311 aa. vCCI uses, residues from its beta-sheet II to interact with a surface of MIP-1beta, that includes residues adjacent to its N terminus, as well as residues in, the 20's region and the 40's loop. This structure reveals the strategy, used by vCCI to tightly bind numerous chemokines while retaining, selectivity for the CC chemokine subfamily.
About this Structure
2FFK is a Protein complex structure of sequences from Homo sapiens and Rabbitpox virus. Full crystallographic information is available from OCA.
Reference
Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta., Zhang L, Derider M, McCornack MA, Jao SC, Isern N, Ness T, Moyer R, LiWang PJ, Proc Natl Acad Sci U S A. 2006 Sep 19;103(38):13985-90. Epub 2006 Sep 8. PMID:16963564
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