1DOA
Structure of the rho family gtp-binding protein cdc42 in complex with the multifunctional regulator rhogdi
Summary for 1DOA
Entry DOI | 10.2210/pdb1doa/pdb |
Descriptor | PROTEIN (GTP-BINDING PROTEIN), PROTEIN (GDP-DISSOCIATION INHIBITOR 1), MAGNESIUM ION, ... (6 entities in total) |
Functional Keywords | gtp-binding protein, cdc42, rhogdi, cell cycle |
Biological source | Homo sapiens (human) More |
Cellular location | Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P60953 Cytoplasm: P19803 |
Total number of polymer chains | 2 |
Total formula weight | 46654.44 |
Authors | Hoffman, G.R.,Nassar, N.,Cerione, R.C. (deposition date: 1999-12-20, release date: 2000-02-09, Last modification date: 2025-03-26) |
Primary citation | Hoffman, G.R.,Nassar, N.,Cerione, R.A. Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell(Cambridge,Mass.), 100:345-356, 2000 Cited by PubMed Abstract: 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. PubMed: 10676816DOI: 10.1016/S0092-8674(00)80670-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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