期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1999
卷号：96
期号：22
页码：12379-12383
DOI：10.1073/pnas.96.22.12379
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Most poxviruses, including variola, the causative agent of smallpox, express a secreted protein of 35 kDa, vCCI, which binds CC-chemokines with high affinity. This viral protein competes with the host cellular CC-chemokine receptors (CCRs), reducing inflammation and interfering with the host immune response. Such proteins or derivatives may have therapeutic uses as anti-inflammatory agents. We have determined the crystal structure to 1.85-A resolution of vCCI from cowpox virus, the prototype of this poxvirus virulence factor. The molecule is a {beta}-sandwich of topology not previously described. A patch of conserved residues on the exposed face of a {beta}-sheet that is strongly negatively charged might have a role in binding of CC-chemokines, which are positively charged.
