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3qcd

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Current revision (11:40, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3qcd' size='340' side='right'caption='[[3qcd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3qcd' size='340' side='right'caption='[[3qcd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qcd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QCD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qcd]] 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=3QCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QCD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qcb|3qcb]], [[3qcc|3qcc]], [[3qce|3qce]], [[3qcf|3qcf]], [[3qcg|3qcg]], [[3qch|3qch]], [[3qci|3qci]], [[3qcj|3qcj]], [[3qck|3qck]], [[3qcl|3qcl]], [[3qcm|3qcm]], [[3qcn|3qcn]]</div></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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPG, PTPRG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://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=3qcd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qcd OCA], [https://pdbe.org/3qcd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qcd RCSB], [https://www.ebi.ac.uk/pdbsum/3qcd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qcd ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qcd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qcd OCA], [https://pdbe.org/3qcd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qcd RCSB], [https://www.ebi.ac.uk/pdbsum/3qcd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qcd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PTPRG_HUMAN PTPRG_HUMAN]] Possesses tyrosine phosphatase activity.<ref>PMID:19167335</ref>
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[https://www.uniprot.org/uniprot/PTPRG_HUMAN PTPRG_HUMAN] Possesses tyrosine phosphatase activity.<ref>PMID:19167335</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein tyrosine phosphatases (PTPs) catalyze the dephosphorylation of tyrosine residues, a process that involves a conserved tryptophan-proline-aspartate (WPD) loop in catalysis. In previously determined structures of PTPs, the WPD-loop has been observed in either an "open" conformation or a "closed" conformation. In the current work, X-ray structures of the catalytic domain of receptor-like protein tyrosine phosphatase gamma (RPTPgamma) revealed a ligand-induced "superopen" conformation not previously reported for PTPs. In the superopen conformation, the ligand acts as an apparent competitive inhibitor and binds in a small hydrophobic pocket adjacent to, but distinct from, the active site. In the open and closed WPD-loop conformations of RPTPgamma, the side chain of Trp1026 partially occupies this pocket. In the superopen conformation, Trp1026 is displaced allowing a 3,4-dichlorobenzyl substituent to occupy this site. The bound ligand prevents closure of the WPD-loop over the active site and disrupts the catalytic cycle of the enzyme.
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Small molecule receptor protein tyrosine phosphatase gamma (RPTPgamma) ligands that inhibit phosphatase activity via perturbation of the tryptophan-proline-aspartate (WPD) loop.,Sheriff S, Beno BR, Zhai W, Kostich WA, McDonnell PA, Kish K, Goldfarb V, Gao M, Kiefer SE, Yanchunas J, Huang Y, Shi S, Zhu S, Dzierba C, Bronson J, Macor JE, Appiah KK, Westphal RS, O'Connell J, Gerritz SW J Med Chem. 2011 Oct 13;54(19):6548-62. Epub 2011 Sep 20. PMID:21882820<ref>PMID:21882820</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 3qcd" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Sheriff S]]
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[[Category: Sheriff, S]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Twisted mixed beta-sheets flanked by {alpha}-helice]]
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[[Category: Tyrosine receptor phosphatase]]
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Current revision

Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate, trigonal crystal form

PDB ID 3qcd

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