Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2
The protein tyrosine phosphatase SHP2 is a key regulator of cell cycle control. Here the authors combine NMR measurements and X-ray crystallography and show that wild-type SHP2 dynamically exchanges between a closed inactive conformation and an open activated form and that the oncogenic E76K mutatio...
Enregistré dans:
Auteurs principaux: | Ricardo A. P. Pádua, Yizhi Sun, Ingrid Marko, Warintra Pitsawong, John B. Stiller, Renee Otten, Dorothee Kern |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2018
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/77cc04b8724e47ce9663728a803fea11 |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Structural reorganization of SHP2 by oncogenic mutations and implications for oncoprotein resistance to allosteric inhibition
par: Jonathan R. LaRochelle, et autres
Publié: (2018) -
Discriminating between competing models for the allosteric regulation of oncogenic phosphatase SHP2 by characterizing its active state
par: Paolo Calligari, et autres
Publié: (2021) -
Lymphocyte cell-cycle inhibition by HLA-G is mediated by phosphatase SHP-2 and acts on the mTOR pathway.
par: Farah Ketroussi, et autres
Publié: (2011) -
Protein tyrosine phosphatase Shp2 deficiency in podocytes attenuates lipopolysaccharide-induced proteinuria
par: Ming-Fo Hsu, et autres
Publié: (2017) -
PD-L2 suppresses T cell signaling via coinhibitory microcluster formation and SHP2 phosphatase recruitment
par: Tomohiro Takehara, et autres
Publié: (2021)