An NMR study of the complex formed by viral protein vCCI and human chemokine eotaxin
EMSL Project ID
25422b
Abstract
Chemokines are essential components of the immune system, causing activation and chemotaxis of leukocytes to sites of infection and inflammation. While the structures of many chemokines are known, data are lacking on the structure of chemokines in complex with their binding partners. One important binding partner is the virally encoded chemokine binding protein, vCCI, that can tightly bind many chemokines as a method of evading the immune response. This 240 amino acid, poxvirus encoded protein behaves as a chemokine scavenger by binding with CC chemokines with very high affinity. With the assistance of PNNL, we have recently completed the first structure determination of vCCI in complex with a chemokine (MIP-1?), and the next phase of our research is to study the ability of vCCI to bind chemokines with direct relevance to allergy and asthma. The chemokine binding partner for vCCI that we have chosen is eotaxin, a protein that helps direct the influx of eosinophils to the asthmatic lung. We have successfully made the vCCI-eotaxin complex and are using NMR to elucidate the interaction between these two proteins. When complete, this work will represent the first structure of eotaxin in complex, and only the second structure of vCCI in complex.
Project Details
Project type
Large-Scale EMSL Research
Start Date
2007-10-22
End Date
2009-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Kuo NW, Y Gao, MS Schill, NG Isern, CM Dupureur, and PJ Liwang. 2014. "Structural Insights into the Interaction Between a Potent Anti-Inflammatory Protein, vCCI, and the Human CC Chemokine, Eotaxin-1." Journal of Biological Chemistry. doi:10.1074/jbc.M113.538991