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NMR <sup>1</sup>H, <sup>13</sup>C, <sup>15</sup>N backbone resonance assignments of the T35S and oncogenic T35S/Q61L mutants of human KRAS4b in the active, GppNHp-bound conformation.


ABSTRACT: RAS proteins cycling between the active-form (GTP-bound) and inactive-form (GDP-bound) play a key role in cell signaling pathways that control cell survival, proliferation, and differentiation. Mutations at codon 12, 13, and 61 in RAS are known to attenuate its GTPase activity favoring the RAS active state and constitutively active downstream signaling. This hyperactivation accounts for various malignancies including pancreatic, lung, and colorectal cancers. Active KRAS is found to exist in equilibrium between two rapidly interconverting conformational states (State1-State2) in solution. Due to this dynamic feature of the protein, the 1H-15N correlation cross-peak signals of several amino acid (AA) residues of KRAS belonging to the flexible loop regions are absent fro

SUBMITTER: Sharma AK 

PROVIDER: S-EPMC9068649 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature