6fsf
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Crystal structure of the tandem PX-PH-domains of Bem3 from Saccharomyces cerevisiae
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Structural highlights
FunctionBEM3_YEAST GTPase-activating protein (GAP) for CDC42 and less efficiently for RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase.[1] [2] Publication Abstract from PubMedThe structure of the tandem lipid-binding PX and pleckstrin-homology (PH) domains of the Cdc42 GTPase-activating protein Bem3 from Saccharomyces cerevisiae (strain S288c) has been determined to a resolution of 2.2 A (Rwork = 21.1%, Rfree = 23.4%). It shows that the domains adopt a relative orientation that enables them to simultaneously bind to a membrane and suggests possible cooperativity in membrane binding. Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae.,Ali I, Eu S, Koch D, Bleimling N, Goody RS, Muller MP Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):315-321. doi:, 10.1107/S2053230X18005915. Epub 2018 Apr 24. PMID:29718000[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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