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 |