GTP-binding protein: Difference between revisions
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== Function == | == Function == | ||
'''GTP-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'''<ref>PMID:14762218</ref> see [[Transducin]] and '''small GTPases'''<ref>PMID:11152757</ref>. 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]]. | '''GTP-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'''<ref>PMID:14762218</ref> see [[Transducin]] and '''small GTPases'''<ref>PMID:11152757</ref>. 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<ref>PMID:24552710</ref>. | ||
'''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<br /> | '''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<br /> | ||
