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
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: | https://repository.cshl.edu/id/eprint/29057 |
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