3qcc: Difference between revisions
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==Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate, orthorhombic crystal form== | ==Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate, orthorhombic crystal form== | ||
<StructureSection load='3qcc' size='340' side='right' caption='[[3qcc]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3qcc' size='340' side='right' caption='[[3qcc]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3qcc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3qcc]] is a 2 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=3QCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QCC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qcb|3qcb]], [[3qcd|3qcd]], [[3qce|3qce]], [[3qcf|3qcf]], [[3qcg|3qcg]], [[3qch|3qch]], [[3qci|3qci]], [[3qcj|3qcj]], [[3qck|3qck]], [[3qcl|3qcl]], [[3qcm|3qcm]], [[3qcn|3qcn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qcb|3qcb]], [[3qcd|3qcd]], [[3qce|3qce]], [[3qcf|3qcf]], [[3qcg|3qcg]], [[3qch|3qch]], [[3qci|3qci]], [[3qcj|3qcj]], [[3qck|3qck]], [[3qcl|3qcl]], [[3qcm|3qcm]], [[3qcn|3qcn]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPG, PTPRG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPG, PTPRG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<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> | <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> | ||
<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=3qcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qcc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qcc RCSB], [http://www.ebi.ac.uk/pdbsum/3qcc PDBsum]</span></td></tr> | <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=3qcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qcc OCA], [http://pdbe.org/3qcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qcc RCSB], [http://www.ebi.ac.uk/pdbsum/3qcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qcc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3qcc" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Sheriff, S]] | [[Category: Sheriff, S]] | ||
Revision as of 18:43, 4 August 2016
Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate, orthorhombic crystal formHuman receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate, orthorhombic crystal form
Structural highlights
Function[PTPRG_HUMAN] Possesses tyrosine phosphatase activity.[1] Publication Abstract from PubMedProtein 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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[[Category: Twisted mixed beta-sheets flanked by {alpha}-helice]]