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

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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Bibliographic Details
Main Authors: Michelangelo Marasco, John Kirkpatrick, Teresa Carlomagno, Jochen S. Hub, Massimiliano Anselmi
Format: Article
Language:English
Published: Elsevier 2024-12-01
Series:Computational and Structural Biotechnology Journal
Subjects:
SHP2 phosphatase
N-SH2 domain
Molecular dynamics simulations
NMR spectroscopy
Allosteric coupling
Protein flexibility
Online Access:http://www.sciencedirect.com/science/article/pii/S2001037024000473

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http://www.sciencedirect.com/science/article/pii/S2001037024000473

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