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Sci. Signal., 17 July 2012
Vol. 5, Issue 233, p. ec191
[DOI: 10.1126/scisignal.2003394]

EDITORS' CHOICE

Structural Biology GPCR Close-Up

Valda Vinson

Science, AAAS, Washington, DC 20005, USA

Structures of G protein–coupled receptors (GPCRs), determined in the past few years, have provided insight into the function of this important family of membrane proteins. Liu et al. used a protein-engineering strategy to produce a stabilized version of the human A2A adenosine receptor (A2AAR). The high-resolution structure reveals the position of about 60 internal waters, which suggests an almost continuous channel in the GPCR and can explain the allosteric effects of Na+ on ligand binding and how cholesterol may contribute to GPCR stabilization.

W. Liu, E. Chun, A. A. Thompson, P. Chubukov, F. Xu, V. Katritch, G. W. Han, C. B. Roth, L. H. Heitman, A. P. IJzerman, V. Cherezov, R. C. Stevens, Structural basis for allosteric regulation of GPCRs by sodium ions. Science 337, 232–236 (2012). [Abstract] [Full Text]

Citation: V. Vinson, GPCR Close-Up. Sci. Signal. 5, ec191 (2012).

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