Application for 800MHz NMR spectrometer time to facilitate the structural study of the complex formed by pox virus encoded protein vCCI and human CC chemokine MIP-1beta
EMSL Project ID
10296
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 242 amino acid, poxvirus encoded protein, vCCI, which can tightly bind chemokines, such as MIP-1, as a method of evading the immune response. We have successfully made the vCCI-MIP-1 complex and are using NMR to elucidate the interaction between these two proteins. Our results show that upon binding, the 15N HSQC spectrum of MIP-1undergoes remarkable changes, suggesting significant conformational rearrangement. vCCI forms a complex with MIP- with 1:1 stoichiometry, indicating that complex formation disrupts the chemokine dimer. We are using multidimensional NMR experiments to acquire information for solving the structure of this complex. When complete, this work will represent the first structure of MIP-1 in complex.
Project Details
Project type
Capability Research
Start Date
2004-12-06
End Date
2005-10-03
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members