1ptu
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CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH PHOSPHOTYROSINE-CONTAINING HEXA-PEPTIDE (DADEPYL-NH2)
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Abdominal body fat distribution, modifier of OMIM:[176885], Insulin resistance, susceptibility to OMIM:[176885]
About this StructureAbout this Structure
1PTU is a Single protein structure of sequence from Homo sapiens with NH2 as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B., Jia Z, Barford D, Flint AJ, Tonks NK, Science. 1995 Jun 23;268(5218):1754-8. PMID:7540771
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