Structure of the Rho Family GTP-Binding Protein Cdc42 in Complex with the Multifunctional Regulator RhoGDI
Copyright policy )Structure of the Rho Family GTP-Binding Protein Cdc42 in Complex with the Multifunctional Regulator RhoGDI
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.
- Cornell University United States
- CORNELL UNIVERSITY ITHACA
- Veterinary Medical Center Japan
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Biochemistry, Genetics and Molecular Biology(all), Surface Properties, Molecular Sequence Data, Protein Prenylation, Membrane Proteins, Crystallography, X-Ray, Guanosine Diphosphate, rho-Specific Guanine Nucleotide Dissociation Inhibitors, Amino Acid Sequence, Diterpenes, cdc42 GTP-Binding Protein, Guanine Nucleotide Dissociation Inhibitors, Protein Binding, Signal Transduction
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Biochemistry, Genetics and Molecular Biology(all), Surface Properties, Molecular Sequence Data, Protein Prenylation, Membrane Proteins, Crystallography, X-Ray, Guanosine Diphosphate, rho-Specific Guanine Nucleotide Dissociation Inhibitors, Amino Acid Sequence, Diterpenes, cdc42 GTP-Binding Protein, Guanine Nucleotide Dissociation Inhibitors, Protein Binding, Signal Transduction
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