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Article

Mutational landscape of K-Ras substitutions at 12th position-a systematic molecular dynamics approach.

Journal of biomolecular structure & dynamics - 1 Mar 2022

S Udhaya Kumar, R Bithia, D Thirumal Kumar, Doss C George Priya, Zayed Hatem

Abstract excerpt

K-Ras is a small GTPase and acts as a molecular switch by recruiting GEFs and GAPs, and alternates between the inert GDP-bound and the dynamic GTP-bound forms. The amino acid at position 12 of K-Ras is a hot spot for oncogenic mutations (G12A, G12C, G12D, G12R, G12S, and G12V), disturbing the active fold of the protein, leading to cancer development. This study aimed to investigate the potential conformational...

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Identifiers

PMID: 33034275
DOI: 10.1080/07391102.2020.1830177

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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