Structural impact of GTP binding on downstream KRAS signaling
Dóra K. Menyhárd, Gyula Pálfy, Zoltán Orgován, István Vida, György M. Keserű, András Perczel
Abstract
widens the pocket. Position 12 mutations do not disturb the capture of Tyr32 by the γ-phosphate, but (partially) displace Gln61, which opens up the catalytic pocket and destabilizes catalytic water molecules thus impairing intrinsic hydrolysis.
Topics & Concepts
KRASGTP'Downstream (manufacturing)NucleotideChemistryGTPaseCell biologySignal transductionComputational biologyBiologyBiochemistryMutationBusinessEnzymeGeneMarketingProtein Kinase Regulation and GTPase SignalingCell death mechanisms and regulationCellular transport and secretion