학술논문

Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state
Document Type
article
Source
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Subject
Science
Language
English
ISSN
2041-1723
Abstract
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.