REVEALING MECHANISMS FOR SH2 DOMAIN MEDIATED REGULATION OF THE PROTEIN-TYROSINE-PHOSPHATASE SHP-2

The crystal structure of the protein tyrosine phosphatase SHP-2 reveal s the mechanism of auto-inhibition of phosphatase activity by its SH2 domains, Phosphotyrosine peptide stimulation of the phosphatase activi ty, resulting from peptide binding to the N-terminal SH2 domain, is li nked to conformational changes within the protein, including an unprec edented allosteric transition of the N-terminal SH2 domain.