Phosphopeptide binding to the N-SH2 domain of tyrosine phosphatase SHP2 correlates with the unzipping of its central β-sheet

SHP2 is a tyrosine phosphatase that plays a regulatory role in multiple intracellular signaling cascades and is known to be oncogenic in certain contexts. In the absence of effectors, SHP2 adopts an autoinhibited conformation with its N-SH2 domain blocking the active site. Given the key role of N-SH...

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Váldodahkkit:	Michelangelo Marasco, John Kirkpatrick, Teresa Carlomagno, Jochen S. Hub, Massimiliano Anselmi
Materiálatiipa:	Artigo
Giella:	Inglês
Almmustuhtton:	American Association for the Advancement of Science (AAAS) 2024-12-01
Ráidu:	Computational and Structural Biotechnology Journal
Fáttát:	SHP2 phosphatase N-SH2 domain Molecular dynamics simulations NMR spectroscopy Allosteric coupling Protein flexibility
Liŋkkat:	http://www.sciencedirect.com/science/article/pii/S2001037024000473
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