Getting to Grips with G Protein Structure

doi:10.1126/stke.3142005tw450

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Sci. STKE, 13 December 2005
Vol. 2005, Issue 314, p. tw450
[DOI: 10.1126/stke.3142005tw450]

EDITORS' CHOICE

STRUCTURAL BIOLOGY Getting to Grips with G Protein Structure

Heterotrimeric G protein signaling is important in a wide range of physiological processes; however, little is known about how activated heterotrimer subunits (G ${alpha}$ ß ${gamma}$ ) are oriented at the membrane during signal transduction. Tesmer et al. provide a snapshot of activated G proteins in a 3.1 angstrom crystal structure of G protein-coupled receptor kinase 2 (GRK2) bound simultaneously to activated G ${alpha}$ _q and Gß ${gamma}$ . GRK2 is critical to the phosphorylation-dependent desensitization of many G protein-coupled receptors. In the complex, G ${alpha}$ _q is fully dissociated from Gß ${gamma}$ , is oriented away from its position in the heterotrimer, and forms an effector-like interaction with GRK2.

V. M. Tesmer, T. Kawano, A. Shankaranarayanan, T. Kozasa, J. J. G. Tesmer, Snapshot of activated G proteins at the membrane: The G ${alpha}$ _q-GRK2-Gß ${gamma}$ complex. Science 310, 1686-1690 (2005). [Abstract] [Full Text]

Citation: Getting to Grips with G Protein Structure. Sci. STKE 2005, tw450 (2005).

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REVIEWS G Protein Signaling: Insights from New Structures: Anita M. Preininger and Heidi E. Hamm (3 February 2004)
Sci. STKE 2004 (218), re3. [DOI: 10.1126/stke.2182004re3]
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