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1doa

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{{STRUCTURE_1doa| PDB=1doa | SCENE= }}
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'''STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI'''
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===STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI===
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==Overview==
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The 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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10676816 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10676816}}
==About this Structure==
==About this Structure==
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[[Category: Rhogdi]]
[[Category: Rhogdi]]
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[[Category: X-ray]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:04:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:22:12 2008''

Revision as of 20:22, 30 June 2008

Template:STRUCTURE 1doa

STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI

Template:ABSTRACT PUBMED 10676816

About this Structure

1DOA is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jun 30 23:22:12 2008

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