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Article

B-Raf autoinhibition in the presence and absence of 14-3-3.

Structure (London, England : 1993) - 1 Jul 2021

Zhang Mingzhen, Jang Hyunbum, Li Zhigang, Sacks David B, Nussinov Ruth

Abstract excerpt

Raf-activating mutations are frequent in cancer. In the basal state, B-Raf is autoinhibited by its upstream Ras-binding domain (RBD) and cysteine-rich domain (RBD-CRD) interacting with its kinase domain (KD) and the 14-3-3 dimer. Our comprehensive molecular dynamics simulations explore two autoinhibition scenarios in the presence and absence of the 14-3-3 dimer. When present, the 14-3-3 interaction with B-Raf...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 33711246
DOI: 10.1016/j.str.2021.02.005
PMCID: PMC9907365

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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