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Article

Allosteric inhibitor remotely modulates the conformation of the orthestric pockets in mutant IDH2/R140Q.

Scientific reports - 28 Nov 2017

Chen Jiao, Yang Jie, Sun Xianqiang, Wang Zhongming, Cheng Xiaolan, Lu Wuguang, Cai Xueting, Hu Chunping, Shen Xu, Cao Peng

Abstract excerpt

Neomorphic mutation R140Q in the metabolic enzyme isocitrate dehydrogenase 2 (IDH2) is found to be a driver mutation in cancers. Recent studies revealed that allosteric inhibitors could selectively inhibit IDH2/R140Q and induce differentiation of TF-1 erythroleukemia and primary human AML cells. However, the allosteric inhibition mechanism is not very clear. Here, we report the results from computational studies...

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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: 29184081
DOI: 10.1038/s41598-017-16427-w
PMCID: PMC5705638

Genes

IDH2

Variants

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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