2FFK

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

2FFK の概要

• エントリーDOI: 10.2210/pdb2ffk/pdb
• 関連するPDBエントリー: 2FIN
• NMR情報: BMRB: 6809
• 分子名称: rabbitpox encoded CC chemokine inhibitor, Small inducible cytokine A4 (2 entities in total)
• 機能のキーワード: protein-protein complex, chemokine, pox virus, viral cc chemokine inhibitor, virus-viral protein-cytokine complex, virus/viral protein/cytokine
• 由来する生物種: Rabbitpox virus; 詳細
• 細胞内の位置: Secreted: P13236
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33780.28

構造登録者

Zhang, L. (登録日: 2005-12-19, 公開日: 2006-08-22, 最終更新日: 2024-11-06)

主引用文献

Zhang, L.,Derider, M.,McCornack, M.A.,Jao, S.C.,Isern, N.,Ness, T.,Moyer, R.,Liwang, P.J.
Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta.
Proc.Natl.Acad.Sci.Usa, 103:13985-13990, 2006

PubMed Abstract: 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.

PubMed: 16963564
DOI: 10.1073/pnas.0602142103

実験手法

SOLUTION NMR