Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK
作者： Helen R. Mott , Darerca Owen , Daniel Nietlispach , Peter N. Lowe , Edward Manser
DOI: 10.1038/20732
关键词: Protein structure 、 Cdc42 GTP-Binding Protein 、 GTP-binding protein regulators 、 Cell biology 、 Biochemistry 、 G protein 、 GTPase-activating protein 、 Effector 、 Small G Protein 、 GTPase 、 Biology
摘要: The proteins Cdc42 and Rac are members of the Rho family small GTPases (G proteins), which control signal-transduction pathways that lead to rearrangements cell cytoskeleton, differentiation proliferation. They do so by binding downstream effector proteins. Some these, known as CRIB (for Cdc42/Rac interactive-binding) proteins, bind both Rac, such PAK1-3 serine/threonine kinases, whereas others specific for Cdc42, ACK tyrosine kinases Wiscott-Aldrich-syndrome (WASPs). loop (comprising residues 30-40, also called switch I), is one two regions change conformation on exchange GDP GTP. This region almost identical in Racs, indicating it does not determine specificity these G Here we report solution structure complex with GTPase-binding domain ofACK. Both undergo significant conformational changes binding, form a new type G-protein/effector complex. interaction extends beta-sheet an extended strand from ACK, seen Ras/effector interactions, but involves other protein important determining binding.
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