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3qkq

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Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate

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Retrieved from "http://52.214.119.220/wiki/index.php/3qkq"

Categories: Homo sapiens | Large Structures | Brandao TAS | Hengge AC | Johnson SJ

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 ==Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate==
-<StructureSection load='3qkq' size='340' side='right' caption='[[3qkq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='3qkq' size='340' side='right'caption='[[3qkq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qkq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cm2|2cm2]], [[3f9b|3f9b]], [[3qkn|3qkn]], [[3qko|3qko]], [[3qkp|3qkp]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ptp1b, ptpn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [https://pdbe.org/3qkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [https://www.ebi.ac.uk/pdbsum/3qkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qkq ProSAT]</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=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [http://www.ebi.ac.uk/pdbsum/3qkq PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The movement of a conserved protein loop (the WPD-loop) is important in catalysis by protein tyrosine phosphatases (PTPs). Using kinetics, isotope effects, and X-ray crystallography, the different effects arising from mutation of the conserved tryptophan in the WPD-loop were compared in two PTPs, the human PTP1B, and the bacterial YopH from Yersinia. Mutation of the conserved tryptophan in the WPD-loop to phenylalanine has a negligible effect on k(cat) in PTP1B and full loop movement is maintained. In contrast, the corresponding mutation in YopH reduces k(cat) by two orders of magnitude and the WPD loop locks in an intermediate position, disabling general acid catalysis. During loop movement the indole moiety of the WPD-loop tryptophan moves in opposite directions in the two enzymes. Comparisons of mammalian and bacterial PTPs reveal differences in the residues forming the hydrophobic pocket surrounding the conserved tryptophan. Thus, although WPD-loop movement is a conserved feature in PTPs, differences exist in the molecular details, and in the tolerance to mutation, in PTP1B compared to YopH. Despite high structural similarity of the active sites in both WPD-loop open and closed conformations, differences are identified in the molecular details associated with loop movement in PTPs from different organisms.
-The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B.,Brandao TA, Johnson SJ, Hengge AC Arch Biochem Biophys. 2012 Sep 1;525(1):53-9. Epub 2012 Jun 12. PMID:22698963<ref>PMID:22698963</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-==See Also==
-*[[Tyrosine phosphatase|Tyrosine phosphatase]]
 == References ==
 <references/>
@@ Line 27: / Line 15: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Brandao, T A.S]]
+[[Category: Brandao TAS]]
-[[Category: Hengge, A C]]
+[[Category: Hengge AC]]
-[[Category: Johnson, S J]]
+[[Category: Johnson SJ]]
-[[Category: Egfr receptor]]
-[[Category: Hydrolase]]
-[[Category: P-loop]]
-[[Category: Phosphoprotein]]
-[[Category: Protein phosphatase]]
-[[Category: Vanadate]]
-[[Category: Wpd-loop]]

3qkq

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Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate

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