Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
摘要：
The crystal structures of a cysteine-215-->serine mutant of protein tyrosine phosphatase 1B complexed with high-affinity peptide substrates corresponding to an autophosphorylation site of the epidermal growth factor receptor were determined. Peptide binding to the protein phosphatase was accompanied by a conformational change of a surface loop that created a phosphotyrosine recognition pocket and induced a catalytically competent form of the enzyme. The phosphotyrosine side chain is buried within the period and anchors the peptide substrate to its binding site. Hydrogen bonds between peptide main-chain atoms and the protein contribute to binding affinity, and specific interactions of acidic residues of the peptide with basic residues on the surface of the enzyme confer sequence specificity.
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关键词：
Tyrosine Phosphotyrosine Oligopeptides Receptor, Epidermal Growth Factor Crystallography, X-Ray Protein Conformation Protein Structure, Secondary Binding Sites Protein Tyrosine Phosphatases Computer Graphics
DOI：
10.1126/science.7540771
被引量：
年份：
1995
Wiley
万方医学
掌桥科研
dx.doi.org
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