NMR ¹H, ¹³C, and ¹⁵N resonance assignments of the oncogenic Q61R variant of human NRAS in the active, GTP-bound conformation.

ABSTRACT: NRAS^Q61R is a frequent mutation in melanoma. Hydrolysis of GTP by NRAS^Q61R is reported to be much slower than other KRAS and NRAS mutants. Recent structural biology efforts for KRAS and NRAS proteins have been limited to X-ray crystallography and therefore lack insight into the structure and dynamics of these proteins in solution. Here we report the ¹H^N, ¹⁵N, and ¹³C backbone and sidechain resonance assignments of the G-domain of oncogenic NRAS^Q61R-GTP (MW 19.3 kDa; aa 1-169) using heteronuclear, multidimensional NMR spectroscopy. NRAS^Q61R-GTP is a conformationally stable protein in solution. The ¹H-¹⁵N correlation cross-peaks in a 2D ¹H-¹⁵N HSQC spectrum coll

SUBMITTER: Sharma AK 

PROVIDER: S-EPMC12116848 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature