Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state.

doi:10.1038/s41467-022-30463-9

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Article

Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state.

Nature communications - 30 Jun 2022

Miller Peter G, Sathappa Murugappan, Moroco Jamie A, Jiang Wei, Qian Yue, Iqbal Sumaiya, Guo Qi, Giacomelli Andrew O, Shaw Subrata, Vernier Camille, Bajrami Besnik, Yang Xiaoping, Raffier Cerise, Sperling Adam S, Gibson Christopher J, Kahn Josephine, Jin Cyrus, Ranaghan Matthew, Caliman Alisha, Brousseau Merissa, Fischer Eric S, Lintner Robert, Piccioni Federica, Campbell Arthur J, Root David E, Garvie Colin W, Ebert Benjamin L

Abstract excerpt

PPM1D encodes a serine/threonine phosphatase that regulates numerous pathways including the DNA damage response and p53. Activating mutations and amplification of PPM1D are found across numerous cancer types. GSK2830371 is a potent and selective allosteric inhibitor of PPM1D, but its mechanism of binding and inhibition of catalytic activity are unknown. Here we use computational, biochemical and functional...

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PMID: 35773251
DOI: 10.1038/s41467-022-30463-9
PMCID: PMC9246869

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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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