| pubmed-article:7540771 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7540771 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:7540771 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:7540771 | lifeskim:mentions | umls-concept:C0070948 | lld:lifeskim |
| pubmed-article:7540771 | lifeskim:mentions | umls-concept:C0908145 | lld:lifeskim |
| pubmed-article:7540771 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7540771 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:7540771 | pubmed:issue | 5218 | lld:pubmed |
| pubmed-article:7540771 | pubmed:dateCreated | 1995-7-27 | lld:pubmed |
| pubmed-article:7540771 | 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. | lld:pubmed |
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| pubmed-article:7540771 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7540771 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7540771 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7540771 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7540771 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7540771 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:7540771 | pubmed:author | pubmed-author:BarfordDD | lld:pubmed |
| pubmed-article:7540771 | pubmed:author | pubmed-author:JinWW | lld:pubmed |
| pubmed-article:7540771 | pubmed:author | pubmed-author:TonksN KNK | lld:pubmed |
| pubmed-article:7540771 | pubmed:author | pubmed-author:FlintA JAJ | lld:pubmed |
| pubmed-article:7540771 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7540771 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:7540771 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:7540771 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7540771 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7540771 | pubmed:pagination | 1754-8 | lld:pubmed |
| pubmed-article:7540771 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7540771 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7540771 | pubmed:articleTitle | Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. | lld:pubmed |
| pubmed-article:7540771 | pubmed:affiliation | Laboratory of Molecular Biophysics, University of Oxford, UK. | lld:pubmed |
| pubmed-article:7540771 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7540771 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7540771 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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