Entry Database : PDB / ID : 2qbr Structure visualization Downloads & linksTitle Crystal structure of ptp1b-inhibitor complex ComponentsTyrosine-protein phosphatase non-receptor type 1 Details Keywords HYDROLASE / PROTEIN-INHIBITOR COMPLEXFunction / homology Function and homology informationFunction Domain/homology Component
regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / positive regulation of receptor catabolic process / insulin receptor recycling / negative regulation of PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane ... regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / positive regulation of receptor catabolic process / insulin receptor recycling / negative regulation of PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane / platelet-derived growth factor receptor-beta signaling pathway / sorting endosome / mitochondrial crista / positive regulation of IRE1-mediated unfolded protein response / regulation of type I interferon-mediated signaling pathway / regulation of endocytosis / non-membrane spanning protein tyrosine phosphatase activity / positive regulation of protein tyrosine kinase activity / peptidyl-tyrosine dephosphorylation / Regulation of IFNA/IFNB signaling / regulation of signal transduction / cellular response to unfolded protein / growth hormone receptor signaling pathway via JAK-STAT / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of signal transduction / Regulation of IFNG signaling / MECP2 regulates neuronal receptors and channels / Growth hormone receptor signaling / endoplasmic reticulum unfolded protein response / positive regulation of JUN kinase activity / Insulin receptor recycling / negative regulation of insulin receptor signaling pathway / ephrin receptor binding / Integrin signaling / protein dephosphorylation / protein-tyrosine-phosphatase / negative regulation of MAP kinase activity / protein phosphatase 2A binding / protein tyrosine phosphatase activity / endosome lumen / insulin receptor binding / Negative regulation of MET activity / negative regulation of ERK1 and ERK2 cascade / receptor tyrosine kinase binding / insulin receptor signaling pathway / actin cytoskeleton organization / early endosome / mitochondrial matrix / cadherin binding / protein kinase binding / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function Protein-tyrosine phosphatase, non-receptor type-1/2 / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine specific protein phosphatases active site. ... Protein-tyrosine phosphatase, non-receptor type-1/2 / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine specific protein phosphatases active site. / Protein-tyrosine phosphatase, active site / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. / Protein-tyrosine phosphatase-like / Alpha-Beta Complex / Alpha Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.3 Å DetailsAuthors Xu, W. CitationJournal : J.Med.Chem. / Year : 2007Title : Structure-based optimization of protein tyrosine phosphatase 1B inhibitors: from the active site to the second phosphotyrosine binding site.
Authors: Wilson, D.P. / Wan, Z.K. / Xu, W.X. / Kirincich, S.J. / Follows, B.C. / Joseph-McCarthy, D. / Foreman, K. / Moretto, A. / Wu, J. / Zhu, M. / Binnun, E. / Zhang, Y.L. / Tam, M. / Erbe, D.V. / ... Authors : Wilson, D.P. / Wan, Z.K. / Xu, W.X. / Kirincich, S.J. / Follows, B.C. / Joseph-McCarthy, D. / Foreman, K. / Moretto, A. / Wu, J. / Zhu, M. / Binnun, E. / Zhang, Y.L. / Tam, M. / Erbe, D.V. / Tobin, J. / Xu, X. / Leung, L. / Shilling, A. / Tam, S.Y. / Mansour, T.S. / Lee, J. Show more 1 items Show less#1: Journal : Bioorg.Med.Chem. / Year : 2006Title : Bicyclic and Tricyclic Thiophenes as Protein Tyrosine Phosphatase 1B Inhibitor
Authors :
Moretto, A.F. / Kirincich, S.J. / Xu, W.X. / Smith, M.J. / Wan, Z.-K. / Wilson, D.P. / Follows, B.C. / Binnun, E. / Joseph-Mccarthy, D. / Foreman, K. / Erbe, D.V. / Zhang, Y.-L. / Tam, S.K. / Tam, S.Y. / Lee, J. History Deposition Jun 18, 2007 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Mar 18, 2008 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Version format complianceRevision 1.2 Feb 21, 2024 Group : Data collection / Database references / Derived calculationsCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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