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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5218
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pubmed:dateCreated |
1995-7-27
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1754-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7540771-Binding Sites,
pubmed-meshheading:7540771-Computer Graphics,
pubmed-meshheading:7540771-Crystallography, X-Ray,
pubmed-meshheading:7540771-Hydrogen Bonding,
pubmed-meshheading:7540771-Models, Molecular,
pubmed-meshheading:7540771-Oligopeptides,
pubmed-meshheading:7540771-Phosphotyrosine,
pubmed-meshheading:7540771-Protein Conformation,
pubmed-meshheading:7540771-Protein Structure, Secondary,
pubmed-meshheading:7540771-Protein Tyrosine Phosphatases,
pubmed-meshheading:7540771-Receptor, Epidermal Growth Factor,
pubmed-meshheading:7540771-Tyrosine
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pubmed:year |
1995
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pubmed:articleTitle |
Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B.
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pubmed:affiliation |
Laboratory of Molecular Biophysics, University of Oxford, UK.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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