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

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Title: Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state
Authors: Peter G. Miller, Murugappan Sathappa, Jamie A. Moroco, Wei Jiang, Yue Qian, Sumaiya Iqbal, Qi Guo, Andrew O. Giacomelli, Subrata Shaw, Camille Vernier, Besnik Bajrami, Xiaoping Yang, Cerise Raffier, Adam S. Sperling, Christopher J. Gibson, Josephine Kahn, Cyrus Jin, Matthew Ranaghan, Alisha Caliman, Merissa Brousseau, Eric S. Fischer, Robert Lintner, Federica Piccioni, Arthur J. Campbell, David E. Root, Colin W. Garvie, Benjamin L. Ebert
Source: Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Publisher Information: Nature Portfolio, 2022.
Publication Year: 2022
Collection: LCC:Science
Subject Terms: Science
More Details: In this work, the authors report a sophisticated combination of genetic, biophysical, and biochemical analyses to identifies the cycling conformational states of PPM1D. The findings reveal how an allosteric inhibitor locks the protein into a conformationally inactive state, and explain the distribution of PPM1D activating mutations in cancer.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2041-1723
Relation: https://doaj.org/toc/2041-1723
DOI: 10.1038/s41467-022-30463-9
Access URL: https://doaj.org/article/a652e8c526fe4774ba3ec46bd6f06545
Accession Number: edsdoj.652e8c526fe4774ba3ec46bd6f06545
Database: Directory of Open Access Journals
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  Data: In this work, the authors report a sophisticated combination of genetic, biophysical, and biochemical analyses to identifies the cycling conformational states of PPM1D. The findings reveal how an allosteric inhibitor locks the protein into a conformationally inactive state, and explain the distribution of PPM1D activating mutations in cancer.
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