Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2

Structure
David Barford, Benjamin G Neel

Abstract

The crystal structure of the protein tyrosine phosphatase SHP-2 reveals the mechanism of auto-inhibition of phosphatase activity by its SH2 domains. Phosphotyrosine peptide stimulation of the phosphatase activity, resulting from peptide binding to the N-terminal SH2 domain, is linked to conformational changes within the protein, including an unprecedented allosteric transition of the N-terminal SH2 domain.

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Citations

Feb 21, 2008·Cancer Metastasis Reviews·Gordon ChanBenjamin G Neel
Jan 22, 2003·Biochemical and Biophysical Research Communications·Dita GratzingerJoseph A Madri
Mar 15, 2001·Current Opinion in Cell Biology·N K Tonks, B G Neel
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May 15, 2002·Trends in Cardiovascular Medicine·Nina L TsakadzeStanley E D'Souza
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Feb 6, 2004·Proceedings of the National Academy of Sciences of the United States of America·Camilla PerssonArne Ostman
Sep 23, 2008·Proceedings of the National Academy of Sciences of the United States of America·Ben A CrokerBruce Alan Beutler
Nov 23, 2006·Antioxidants & Redox Signaling·Paola Chiarugi, Francesca Buricchi
Dec 14, 1999·Molecular and Cellular Biology·A M O'ReillyB G Neel
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Aug 15, 2003·Molecular and Cellular Biology·Christopher C StebbinsEric O Long
Jun 1, 2004·Molecular and Cellular Biology·Maria I KontaridisAnton M Bennett
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Jun 25, 2008·Blood·Emmanuelle Fourmentraux-NevesAnne Caignard

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