Title : Allosteric KRas4B Can Modulate SOS1 Fast and Slow Ras Activation Cycles.

Pub. Date : 2018 Aug 21

PMID : 30097175






4 Functional Relationships(s)
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1 Our simulations indicate that KRas4B-GTP interacts with the REM allosteric site more strongly than with the CDC25 catalytic site, consistent with its allosteric role in the GDP-to-GTP exchange. Guanosine Triphosphate KRAS proto-oncogene, GTPase Homo sapiens
2 The conformational change facilitates loading KRas4B-GDP at the catalytic site and opening the KRas4B nucleotide-binding site for GDP release and GTP binding. Guanosine Triphosphate KRAS proto-oncogene, GTPase Homo sapiens
3 The conformational change facilitates loading KRas4B-GDP at the catalytic site and opening the KRas4B nucleotide-binding site for GDP release and GTP binding. Guanosine Triphosphate KRAS proto-oncogene, GTPase Homo sapiens
4 GTP binding reduces the affinity of KRas4B-GTP to the CDC25 catalytic site, resulting in its release. Guanosine Triphosphate KRAS proto-oncogene, GTPase Homo sapiens