3d9c

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==Crystal Structure PTP1B complex with aryl Seleninic acid==
==Crystal Structure PTP1B complex with aryl Seleninic acid==
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<StructureSection load='3d9c' size='340' side='right' caption='[[3d9c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='3d9c' size='340' side='right'caption='[[3d9c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3d9c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D9C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3d9c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D9C FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZYZ:(4-{(2S)-2-[(TERT-BUTOXYCARBONYL)AMINO]-3-METHOXY-3-OXOPROPYL}PHENYL)METHANESELENINIC+ACID'>ZYZ</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPN1, PTP1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZYZ:(4-{(2S)-2-[(TERT-BUTOXYCARBONYL)AMINO]-3-METHOXY-3-OXOPROPYL}PHENYL)METHANESELENINIC+ACID'>ZYZ</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d9c OCA], [https://pdbe.org/3d9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d9c RCSB], [https://www.ebi.ac.uk/pdbsum/3d9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d9c ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3d9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d9c OCA], [http://pdbe.org/3d9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d9c RCSB], [http://www.ebi.ac.uk/pdbsum/3d9c PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN]] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
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[https://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d9/3d9c_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d9/3d9c_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3d9c ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3d9c ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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A homotyrosine based seleninic acid irreversibly inhibits protein tyrosine phosphatases by forming a covalent selenosulfide linkage with the active site cysteine sulfhydryl specifically. The details of the event are revealed by model synthetic studies and by kinetic, mass spectrometric, and crystallographic characterization.
 
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Seleninate in place of phosphate: irreversible inhibition of protein tyrosine phosphatases.,Abdo M, Liu S, Zhou B, Walls CD, Wu L, Knapp S, Zhang ZY J Am Chem Soc. 2008 Oct 8;130(40):13196-7. Epub 2008 Sep 10. PMID:18781746<ref>PMID:18781746</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3d9c" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Tyrosine phosphatase|Tyrosine phosphatase]]
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Large Structures]]
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[[Category: Abdo, M]]
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[[Category: Abdo M]]
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[[Category: Knapp, S]]
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[[Category: Knapp S]]
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[[Category: Liu, S]]
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[[Category: Liu S]]
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[[Category: Walls, C D]]
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[[Category: Walls CD]]
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[[Category: Zhang, Z Y]]
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[[Category: Zhang Z-Y]]
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[[Category: Zhou, B]]
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[[Category: Zhou B]]
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[[Category: Covalent bond]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Membrane]]
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[[Category: Oxidation]]
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[[Category: Phosphoprotein]]
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[[Category: Protein phosphatase]]
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Current revision

Crystal Structure PTP1B complex with aryl Seleninic acid

PDB ID 3d9c

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