GTP-binding protein
ContentsFunctionGTP-binding proteins or G proteins are transmitting signals outside the cell which cause changes within the cell. They act as molecular switches which are on when binding GTP and off when binding GDP. GTP-binding proteins belong to two families: heterotrimeric G proteins[1] see Transducin and small GTPases[2]. The structure of small GTPase is homologous to that of the α subunit of heterotrimeric G protein. See details on small GTP-binding protein LepA in LepA. Nucleolar GTP-binding proteins are involved in the biogenesis of ribosome[3]. Heterotrimeric G protein or guanine nucleotide-binding protein or G protein (GNBP) are heterodimeric membrane proteins composed of α, β and γ subunits. GNBP is involved in mammalian cellular signaling pathways. GNBP α subunit binds GDP or GTP. When bound to GTP it dissociates from the β and γ subunits, binds to adenylate cyclase which converts ATP to cAMP. See also G protein-coupled receptor DiseaseMutations in heterotrimeric G protein α subunit were identified in endocrine tumors and in McCune-Albright syndrome[4]. RelevanceRho-related small GTP-binding protein is inhibited by the antifungal drug Cancidas[5]. Structural highlightsE. coli small GTPase ERA binds GDP in a cavity formed by 7 highly conserved regions G1, G4, G5[6]. GDP binding site. Water molecules are shown as red spheres. 3D Structures of GTP-binding proteinGTP-binding protein 3D structures
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Alexander Berchansky, Wayne Decatur, Joel L. Sussman, Jaime Prilusky, Michal Harel