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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...

Journal Title: Nature Communications 01 October 2018, Vol.9(1), pp.1-14
Main Author: Ricardo A. P. Pádua
Other Authors: Yizhi Sun , Ingrid Marko , Warintra Pitsawong , John B. Stiller , Renee Otten , Dorothee Kern
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 2041-1723 ; DOI: 10.1038/s41467-018-06814-w
Zum Text:
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recordid: doaj_soai_doaj_org_article_50572d79c0104cb6be8ad0381f8d3ee6
title: Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2
format: Article
creator:
  • Ricardo A. P. Pádua
  • Yizhi Sun
  • Ingrid Marko
  • Warintra Pitsawong
  • John B. Stiller
  • Renee Otten
  • Dorothee Kern
subjects:
  • Biology
ispartof: Nature Communications, 01 October 2018, Vol.9(1), pp.1-14
description: 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...
language: eng
source:
identifier: E-ISSN: 2041-1723 ; DOI: 10.1038/s41467-018-06814-w
fulltext: fulltext_linktorsrc
issn:
  • 2041-1723
  • 20411723
url: Link


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titleMechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2
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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...

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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...

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