Structural highlights
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
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.
Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus.,Carfi A, Smith CA, Smolak PJ, McGrew J, Wiley DC Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12379-83. PMID:10535930[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carfi A, Smith CA, Smolak PJ, McGrew J, Wiley DC. Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12379-83. PMID:10535930
