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Article

Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin.

Cell - 29 Oct 2004

Canagarajah Bertram, Leskow Federico Coluccio, Ho Jonathan Yew Seng, Mischak Harald, Saidi Layla F, Kazanietz Marcelo G, Hurley James H

Abstract excerpt

The lipid second messenger diacylglycerol acts by binding to the C1 domains of target proteins, which translocate to cell membranes and are allosterically activated. Here we report the crystal structure at 3.2 A resolution of one such protein, beta2-chimaerin, a GTPase-activating protein for the small GTPase Rac, in its inactive conformation. The structure shows that in the inactive state, the N terminus of...

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Identifiers

PMID: 15507211
DOI: 10.1016/j.cell.2004.10.012

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin.PMID 15507211Read ↗

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