Structural basis for the selective activation of Rho GTPases by Dbl exchange factors

Activation of Rho-family GTPases involves the removal of bound GDP and the subsequent loading of GTP, all catalyzed by guanine nucleotide exchange factors (GEFs) of the Dbl-family. Despite high sequence conservation among Rho GTPases, Dbl proteins possess a wide spectrum of discriminatory potentials...

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Veröffentlicht in:	NAT. STRUCT. MOL. BIOL 2002-06, Vol.9 (6), p.468-475
Hauptverfasser:	Sondek, John, Snyder, Jason T, Worthylake, David K, Rossman, Kent L, Betts, Laurie, Pruitt, Wendy M, Siderovski, David P, Der, Channing J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence BASIC BIOLOGICAL SCIENCES Biochemistry Biological Microscopy Biomedical and Life Sciences cdc42 GTP-Binding Protein - chemistry cdc42 GTP-Binding Protein - metabolism CHEMICAL ACTIVATION Crystallography, X-Ray Enzyme Activation ENZYME ACTIVITY GTP-ASES Guanine Nucleotide Exchange Factors - chemistry Guanine Nucleotide Exchange Factors - metabolism Guanosine Triphosphate - metabolism Humans Life Sciences Membrane Biology Models, Molecular Molecular Sequence Data MORPHOLOGY national synchrotron light source Protein Structure Protein Structure, Secondary Protein Structure, Tertiary Proteins - chemistry Proteins - metabolism Proto-Oncogene Proteins - chemistry rac1 GTP-Binding Protein - chemistry rac1 GTP-Binding Protein - metabolism rho GTP-Binding Proteins - chemistry rho GTP-Binding Proteins - metabolism rhoA GTP-Binding Protein - chemistry rhoA GTP-Binding Protein - metabolism Sequence Alignment Structure-Activity Relationship Substrate Specificity T-Lymphoma Invasion and Metastasis-inducing Protein 1
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