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-1β (macrophage inflammatory protein 1β). vCCI binds to the chemokine with 1:1 stoichiometry, forming a complex of 311 aa. vCCI uses residues from its β-sheet II to interact with a surface of MIP-1β 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.
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Dates
Type | When |
---|---|
Created | 18 years, 11 months ago (Sept. 8, 2006, 9 p.m.) |
Deposited | 2 years, 3 months ago (May 8, 2023, 4:10 p.m.) |
Indexed | 11 months, 4 weeks ago (Aug. 28, 2024, 9:08 a.m.) |
Issued | 18 years, 11 months ago (Sept. 19, 2006) |
Published | 18 years, 11 months ago (Sept. 19, 2006) |
Published Online | 18 years, 11 months ago (Sept. 19, 2006) |
Published Print | 18 years, 11 months ago (Sept. 19, 2006) |
@article{Zhang_2006, title={Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1β}, volume={103}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0602142103}, DOI={10.1073/pnas.0602142103}, number={38}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Zhang, Li and DeRider, Michele and McCornack, Melissa A. and Jao, Shu-chuan and Isern, Nancy and Ness, Traci and Moyer, Richard and LiWang, Patricia J.}, year={2006}, month=sep, pages={13985–13990} }