Entry | Database: PDB / ID: 2bgd |
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Title | Structure-based design of Protein Tyrosine Phosphatase-1B Inhibitors |
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Components | PROTEIN-TYROSINE PHOSPHATASE NON-RECEPTOR TYPE 1 |
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Keywords | HYDROLASE / PROTEIN TYROSINE PHOSPHATASE / 1 / 2 / 5-THIADIAZOLIDIN-3-ONE-1 / 1-DIOXIDE TEMPLATE |
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Function / homology | Function and homology information
PTK6 Down-Regulation / regulation of hepatocyte growth factor receptor signaling pathway / positive regulation of receptor catabolic process / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / insulin receptor recycling / negative regulation of vascular endothelial growth factor receptor signaling pathway / positive regulation of IRE1-mediated unfolded protein response / negative regulation of PERK-mediated unfolded protein response / IRE1-mediated unfolded protein response / regulation of intracellular protein transport ...PTK6 Down-Regulation / regulation of hepatocyte growth factor receptor signaling pathway / positive regulation of receptor catabolic process / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / insulin receptor recycling / negative regulation of vascular endothelial growth factor receptor signaling pathway / positive regulation of IRE1-mediated unfolded protein response / negative regulation of PERK-mediated unfolded protein response / IRE1-mediated unfolded protein response / regulation of intracellular protein transport / cytoplasmic side of endoplasmic reticulum membrane / sorting endosome / mitochondrial crista / platelet-derived growth factor receptor-beta signaling pathway / regulation of type I interferon-mediated signaling pathway / regulation of endocytosis / positive regulation of protein tyrosine kinase activity / non-membrane spanning protein tyrosine phosphatase activity / peptidyl-tyrosine dephosphorylation / Regulation of IFNA/IFNB signaling / cellular response to unfolded protein / regulation of signal transduction / 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 / negative regulation of MAP kinase activity / positive regulation of JUN kinase activity / negative regulation of insulin receptor signaling pathway / Insulin receptor recycling / ephrin receptor binding / protein dephosphorylation / Integrin signaling / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / protein phosphatase 2A binding / 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 / cytosol / cytoplasmSimilarity 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 ...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 BetaSimilarity search - Domain/homology |
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Biological species | HOMO SAPIENS (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å |
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Authors | Black, E. / Breed, J. / Breeze, A.L. / Embrey, K. / Garcia, R. / Gero, T.W. / Godfrey, L. / Kenny, P.W. / Morley, A.D. / Minshull, C.A. ...Black, E. / Breed, J. / Breeze, A.L. / Embrey, K. / Garcia, R. / Gero, T.W. / Godfrey, L. / Kenny, P.W. / Morley, A.D. / Minshull, C.A. / Pannifer, A.D. / Read, J. / Rees, A. / Russell, D.J. / Toader, D. / Tucker, J. |
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Citation | Journal: Bioorg.Med.Chem.Lett. / Year: 2005 Title: Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors Authors: Black, E. / Breed, J. / Breeze, A.L. / Embrey, K. / Garcia, R. / Gero, T.W. / Godfrey, L. / Kenny, P.W. / Morley, A.D. / Minshull, C.A. / Pannifer, A.D. / Read, J. / Rees, A. / Russell, D.J. ...Authors: Black, E. / Breed, J. / Breeze, A.L. / Embrey, K. / Garcia, R. / Gero, T.W. / Godfrey, L. / Kenny, P.W. / Morley, A.D. / Minshull, C.A. / Pannifer, A.D. / Read, J. / Rees, A. / Russell, D.J. / Toader, D. / Tucker, J. |
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History | Deposition | Dec 21, 2004 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | May 4, 2005 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jul 13, 2011 | Group: Advisory / Refinement description / Version format compliance |
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Revision 1.2 | Sep 16, 2015 | Group: Source and taxonomy |
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Revision 1.3 | Jul 24, 2019 | Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site |
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Revision 1.4 | May 8, 2024 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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