1CQ3

STRUCTURE OF A SOLUBLE SECRETED CHEMOKINE INHIBITOR, VCCI, FROM COWPOX VIRUS

Summary for 1CQ3

• Entry DOI: 10.2210/pdb1cq3/pdb
• Descriptor: VIRAL CHEMOKINE INHIBITOR (2 entities in total)
• Functional Keywords: beta sandwich, chemokine, cytokine
• Biological source: Cowpox virus
• Total number of polymer chains: 2
• Total formula weight: 50766.07

Authors

Carfi, A.,Smith, C.A.,Smolak, P.J.,McGrew, J.,Wiley, D.C. (deposition date: 1999-08-05, release date: 1999-11-12, Last modification date: 2024-10-16)

Primary citation

Carfi, A.,Smith, C.A.,Smolak, P.J.,McGrew, J.,Wiley, D.C.
Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus.
Proc.Natl.Acad.Sci.USA, 96:12379-12383, 1999

PubMed Abstract: 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.

PubMed: 10535930
DOI: 10.1073/pnas.96.22.12379

Experimental method

X-RAY DIFFRACTION (1.85 Å)