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

D Barford, BG Neel - Structure, 1998 - cell.com
Structure, 1998cell.com
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.
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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