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Article

Hotspot mutations in KIT receptor differentially modulate its allosterically coupled conformational dynamics: impact on activation and drug sensitivity.

PLoS computational biology - 1 Jul 2014

Chauvot de Beauchêne Isaure, Allain Ariane, Panel Nicolas, Laine Elodie, Trouvé Alain, Dubreuil Patrice, Tchertanov Luba

Abstract excerpt

Receptor tyrosine kinase KIT controls many signal transduction pathways and represents a typical allosterically regulated protein. The mutation-induced deregulation of KIT activity impairs cellular physiological functions and causes serious human diseases. The impact of hotspots mutations (D816H/Y/N/V and V560G/D) localized in crucial regulatory segments, the juxtamembrane region (JMR) and the activation (A-)...

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Share to Allosteric Regulation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Hydrogen Bonding

Share to Molecular Dynamics Simulation

Share to Protein Structure, Tertiary

Share to Proto-Oncogene Proteins c-kit

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Source

Open in PubMed Open full text

Identifiers

PMID: 25079768
DOI: 10.1371/journal.pcbi.1003749
PMCID: PMC4117417

Genes

KIT

Provenance

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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Hotspot mutations in KIT receptor differentially modulate its allosterically coupled conformational dynamics: impact on activation and drug sensitivity.PMID 25079768Read ↗

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