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From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BEM3_YEAST BEM3_YEAST]] GTPase-activating protein (GAP) for CDC42 and less efficiently for RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase.<ref>PMID:8227021</ref> <ref>PMID:8300560</ref> | [[http://www.uniprot.org/uniprot/BEM3_YEAST BEM3_YEAST]] GTPase-activating protein (GAP) for CDC42 and less efficiently for RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase.<ref>PMID:8227021</ref> <ref>PMID:8300560</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 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. | ||
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| + | 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<ref>PMID:29718000</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6fsf" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:36, 9 May 2018
Crystal structure of the tandem PX-PH-domains of Bem3 from Saccharomyces cerevisiae
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Categories: Ali, I | Bleimling, N | Eu, S | Goody, R S | Koch, D | Mueller, M P | Bem3 | Endocytosis | Ph domain | Phosphatidylinositol phosphate | Phox | Pip | Pleckstrin homology | Px domain
