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.
MeSH terms
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Enzyme Activation
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Intracellular Signaling Peptides and Proteins
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Models, Molecular
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Protein Conformation
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases / chemistry*
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Protein Tyrosine Phosphatases / metabolism*
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SH2 Domain-Containing Protein Tyrosine Phosphatases
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Signal Transduction
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src Homology Domains*
Substances
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Intracellular Signaling Peptides and Proteins
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases
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SH2 Domain-Containing Protein Tyrosine Phosphatases