2fin | pdb_00002fin

Solution Structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta, ensemble structure

spinqualitylabelsall models 2fin Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fin is a 2 chain structure with sequence from Homo sapiens and Rabbitpox virus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 15 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O10647_9POXV Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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