PerspectiveStructural Biology

A New Bundle of Prospects for Blocking HIV-1 Entry

Science  20 Sep 2013:
Vol. 341, Issue 6152, pp. 1347-1348
DOI: 10.1126/science.1245384

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Summary

Undulating seven times across the cell surface, thus positioning its aminoterminal head and three humps outside and three other humps and its carboxyterminal tail inside the cell, a G protein–coupled receptor (GPCR) may conjure up images of the Loch Ness monster. But unlike Nessie, GPCRs are ubiquitous, mediating physiological functions from vision and smell to fight-or-flight responses and inflammation. Only a few high-resolution structures of GPCRs are available (1, 2). The main HIV-1 co-receptors, CXCR4 (C-X-C chemokine receptor type 4) and CCR5 (C-C chemokine receptor type 5) are GPCRs. Wu et al. previously solved the structure of CXCR4 (1). On page 1387 of this issue, Tan et al. (3) present a 2.7 Å–resolution crystal structure of CCR5, the co-receptor most frequently used by HIV-1 strains for entry into the cell.