2FIN

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

Summary for 2FIN

• Entry DOI: 10.2210/pdb2fin/pdb
• Related: 2FFK
• NMR Information: BMRB: 6809
• Descriptor: rabbitpox encoded CC chemokine inhibitor, Small inducible cytokine A4 (2 entities in total)
• Functional Keywords: protein-protein complex, chemokine, pox virus, viral cc chemokine inhibitor, virus-viral protein-cytokine complex, virus/viral protein/cytokine
• Biological source: Rabbitpox virus; More
• Cellular location: Secreted: P13236
• Total number of polymer chains: 2
• Total formula weight: 33780.28

Authors

Zhang, L. (deposition date: 2005-12-29, release date: 2006-08-22, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

SOLUTION NMR