1doa: Difference between revisions
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Cerione, R C | [[Category: Cerione, R C]] | ||
[[Category: Hoffman, G R | [[Category: Hoffman, G R]] | ||
[[Category: Nassar, N | [[Category: Nassar, N]] | ||
[[Category: Cdc42]] | [[Category: Cdc42]] | ||
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
[[Category: Gtp-binding protein]] | [[Category: Gtp-binding protein]] | ||
[[Category: Rhogdi]] | [[Category: Rhogdi]] |
Revision as of 22:35, 22 December 2014
Structure of the rho family gtp-binding protein cdc42 in complex with the multifunctional regulator rhogdiStructure of the rho family gtp-binding protein cdc42 in complex with the multifunctional regulator rhogdi
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe RhoGDI proteins serve as key multifunctional regulators of Rho family GTP-binding proteins. The 2.6 A X-ray crystallographic structure of the Cdc42/RhoGDI complex reveals two important sites of interaction between GDI and Cdc42. First, the amino-terminal regulatory arm of the GDI binds to the switch I and II domains of Cdc42 leading to the inhibition of both GDP dissociation and GTP hydrolysis. Second, the geranylgeranyl moiety of Cdc42 inserts into a hydrophobic pocket within the immunoglobulin-like domain of the GDI molecule leading to membrane release. The structural data demonstrate how GDIs serve as negative regulators of small GTP-binding proteins and how the isoprenoid moiety is utilized in this critical regulatory interaction. Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI.,Hoffman GR, Nassar N, Cerione RA Cell. 2000 Feb 4;100(3):345-56. PMID:10676816[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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