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

File:1doa.gif


PDB ID 1doa

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, resolution 2.60Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

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

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