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dc.contributor.authorYang, Jian
dc.contributor.authorLiang, Xiaoshan
dc.contributor.authorNiu, Tian-Qi
dc.contributor.authorMeng, Wuyi
dc.contributor.authorZhao, Zhizhuang Joe
dc.contributor.authorZhou, G. Wayne
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:06Z
dc.date.available2022-08-23T16:54:06Z
dc.date.issued1998-10-17
dc.date.submitted2008-08-04
dc.identifier.citation<p>J Biol Chem. 1998 Oct 23;273(43):28199-207.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.273.43.28199
dc.identifier.pmid9774441
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42422
dc.description.abstractThe crystal structures of the protein-tyrosine phosphatase SHP-1 catalytic domain and the complex it forms with the substrate analogue tungstate have been determined and refined to crystallographic R values of 0.209 at 2.5 A resolution and 0.207 at 2.8 A resolution, respectively. Despite low sequence similarity, the catalytic domain of SHP-1 shows high similarity in secondary and tertiary structures with other protein-tyrosine phosphatases (PTPs). In contrast to the conformational changes observed in the crystal structures of PTP1B and Yersinia PTP, the WPD loop (Trp419-Pro428) in the catalytic domain of SHP-1 moves away from the substrate binding pocket after binding the tungstate ion. Sequence alignment and structural analysis suggest that the residues in the WPD loop, especially the amino acid following Asp421, are critical for the movement of WPD loop on binding substrates and the specific activity of protein-tyrosine phosphatases. Our mutagenesis and kinetic measurements have supported this hypothesis.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9774441&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.273.43.28199
dc.subjectAmino Acid Sequence
dc.subjectBacterial Proteins
dc.subjectBinding Sites
dc.subjectCatalytic Domain
dc.subjectCrystallography, X-Ray
dc.subjectElectrostatics
dc.subjectHydrogen Bonding
dc.subjectIntracellular Signaling Peptides and Proteins
dc.subjectKinetics
dc.subjectModels, Molecular
dc.subjectMolecular Sequence Data
dc.subjectPeptide Fragments
dc.subjectProtein Structure, Secondary
dc.subjectProtein Structure, Tertiary
dc.subjectProtein Tyrosine Phosphatase, Non-Receptor Type 11
dc.subjectProtein Tyrosine Phosphatase, Non-Receptor Type 6
dc.subjectProtein Tyrosine Phosphatases
dc.subjectRecombinant Proteins
dc.subjectSequence Homology, Amino Acid
dc.subjectSurface Properties
dc.subjectTungsten Compounds
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleCrystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1
dc.typeArticle
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume273
dc.source.issue43
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/773
dc.identifier.contextkey564688
html.description.abstract<p>The crystal structures of the protein-tyrosine phosphatase SHP-1 catalytic domain and the complex it forms with the substrate analogue tungstate have been determined and refined to crystallographic R values of 0.209 at 2.5 A resolution and 0.207 at 2.8 A resolution, respectively. Despite low sequence similarity, the catalytic domain of SHP-1 shows high similarity in secondary and tertiary structures with other protein-tyrosine phosphatases (PTPs). In contrast to the conformational changes observed in the crystal structures of PTP1B and Yersinia PTP, the WPD loop (Trp419-Pro428) in the catalytic domain of SHP-1 moves away from the substrate binding pocket after binding the tungstate ion. Sequence alignment and structural analysis suggest that the residues in the WPD loop, especially the amino acid following Asp421, are critical for the movement of WPD loop on binding substrates and the specific activity of protein-tyrosine phosphatases. Our mutagenesis and kinetic measurements have supported this hypothesis.</p>
dc.identifier.submissionpathoapubs/773
dc.contributor.departmentDepartment of Pharmacology and Molecular Toxicology
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages28199-207


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