Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B

Jia, Z. C., Barford, D., Flint, A. J., Tonks, N. K. (June 1995) Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science, 268 (5218). pp. 1754-1758. ISSN 0036-8075

URL: http://www.ncbi.nlm.nih.gov/pubmed/7540771
DOI: 10.1126/science.7540771

Abstract

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 protein 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.

Item Type: Paper
Uncontrolled Keywords: HUMAN-PLACENTA MAP KINASE SPECIFICITY PHOSPHORYLATION PURIFICATION DOMAIN LAR
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: June 1995
Date Deposited: 18 Dec 2013 14:59
Last Modified: 18 Dec 2013 14:59
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29057

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