Editors' ChoiceStructural Biology

CCR5-Maraviroc Structure

Sci. Signal.  24 Sep 2013:
Vol. 6, Issue 294, pp. ec231
DOI: 10.1126/scisignal.2004742

The chemokine receptor CCR5, a G protein–coupled receptor best known as a co-receptor during HIV-1 infection, is important in a variety of physiological processes. Tan et al. (see the Perspective by Klasse) now report the high-resolution crystal structure of CCR5 bound to the HIV-1 entry inhibitor maraviroc. The structure suggests that maraviroc acts as a noncompetitive inhibitor by binding to a region of CCR5 that is distinct from the binding site of HIV-1 and chemokines. Comparison of the structure of CCR5 with the other HIV-1 co-receptor, the chemokine receptor CXCR4, provides insight into the co-receptor selectivity of the virus.

Q. Tan, Y. Zhu, J. Li, Z. Chen, G. W. Han, I. Kufareva, T. Li, L. Ma, G. Fenalti, J. Li, W. Zhang, X. Xie, H. Yang, H. Jiang, V. Cherezov, H. Liu, R. C. Stevens, Q. Zhao, B. Wu, Structure of the CCR5 chemokine receptor–HIV entry inhibitor maraviroc complex. Science 341, 1387–1390 (2013). [Abstract] [Full Text]

P. J. Klasse, A new bundle of prospects for blocking HIV-1 entry. Science 341, 1347–1348 (2013). [Abstract] [Full Text]