Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data

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Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data

A team of RR investigators, Xu Wang, Caroline Watson, Joshua S. Sharp, James H. Prestegard, has joined with Tracy M. Handel from UCSD, to pursue a driving biomedical project directed at understanding how glycosaminoglycans (GAGs) help regulate immune cell migration and chemokine signaling. The chemokine, CCL5 or RANTES, aids recruitment and induces endothelial transmigration of T-cells. The receptor for CCL5 also functions as a co-receptor for the aids virus adding to the interest in this project. The team employed a combination of NMR, SAXS and MS techniques to provide a structural model for CCL5 oligomerization. The model shows an extended GAG binding site and suggests a means by which simultaneous GAG binding and receptor interaction may aid cell migration.

Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data. Xu Wang, Caroline Watson, Joshua S. Sharp, Tracy M. Handel, and James H. Prestegard.Structure (2011) 19:1138-1148DOI: 10.1038/nsmb.1853

Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data.
Xu Wang, Caroline Watson, Joshua S. Sharp, Tracy M. Handel, and James H. Prestegard.
Structure (2011) 19:1138-1148
DOI:
10.1038/nsmb.1853