1pty: Difference between revisions

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-[[Image:1pty.png|left|200px]]
-{{STRUCTURE_1pty|  PDB=1pty  |  SCENE=  }}
+==CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH TWO PHOSPHOTYROSINE MOLECULES==
+<StructureSection load='1pty' size='340' side='right'caption='[[1pty]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-===CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH TWO PHOSPHOTYROSINE MOLECULES===
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1pty]] 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=1PTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PTY FirstGlance]. <br>
-{{ABSTRACT_PUBMED_9391040}}
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
-==About this Structure==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pty OCA], [https://pdbe.org/1pty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pty RCSB], [https://www.ebi.ac.uk/pdbsum/1pty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pty ProSAT]</span></td></tr>
-[[1pty]] is a 1 chain structure of [[Tyrosine phosphatase]] 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=1PTY OCA].
+</table>
+== Function ==
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pt/1pty_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1pty ConSurf].
+<div style="clear:both"></div>
 ==See Also==
-*[[Tyrosine phosphatase|Tyrosine phosphatase]]
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:009391040</ref><ref group="xtra">PMID:011917145</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Almo, S C.]]
+[[Category: Almo SC]]
-[[Category: Lawrence, D.]]
+[[Category: Lawrence D]]
-[[Category: Puius, Y A.]]
+[[Category: Puius YA]]
-[[Category: Sullivan, M.]]
+[[Category: Sullivan M]]
-[[Category: Zhang, Z Y.]]
+[[Category: Zhang Z-Y]]
-[[Category: Zhao, Y.]]
+[[Category: Zhao Y]]
-[[Category: Hydrolase]]
-[[Category: Inhibition]]
-[[Category: Phosphorylation]]