Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. Signal., 25 November 2008
Vol. 1, Issue 47, p. ec409
[DOI: 10.1126/scisignal.147ec409]

EDITORS' CHOICE

Biochemistry GPCR Structural Diversity

Valda J. Vinson

Science, AAAS, Washington, DC 20005, USA

G protein–coupled receptors (GPCRs) respond to diverse extracellular signals to activate different signaling pathways. They are important pharmacological targets, but, so far, structural information that might aid drug design is limited to the rhodopsin and adrenergic receptors, and determinants of ligand binding specificity among different GPCRs are unclear. Now Jaakola et al. report the structure of the human A2A adenosine receptor, a receptor that is blocked by caffeine, in complex with an antagonist. The binding pocket is distinct from that in the rhodopsin and adrenergic receptors, suggesting that, rather than a conserved binding pocket with specific amino acid side chains determining specificity, the GPCR binding pocket itself can vary in position and orientation.

V.-P. Jaakola, M. T. Griffith, M. A. Hanson, V. Cherezov, E. Y. T. Chien, J. R. Lane, A. P. IJzerman, R. C. Stevens, The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322, 1211–1217 (2008). [Abstract] [Full Text]

Citation: V. J. Vinson, GPCR Structural Diversity. Sci. Signal. 1, ec409 (2008).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882