3eu0: Difference between revisions

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-{{Seed}}
-[[Image:3eu0.png|left|200px]]
-<!--
+==Crystal structure of the S-nitrosylated Cys215 of PTP1B==
-The line below this paragraph, containing "STRUCTURE_3eu0", creates the "Structure Box" on the page.
+<StructureSection load='3eu0' size='340' side='right'caption='[[3eu0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3eu0]] 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=3EU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EU0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</scene></td></tr>
-{{STRUCTURE_3eu0|  PDB=3eu0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eu0 OCA], [https://pdbe.org/3eu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eu0 RCSB], [https://www.ebi.ac.uk/pdbsum/3eu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eu0 ProSAT]</span></td></tr>
+</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/eu/3eu0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3eu0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein S-nitrosylation mediated by cellular nitric oxide (NO) plays a primary role in executing biological functions in cGMP-independent NO signaling. Although S-nitrosylation appears similar to Cys oxidation induced by reactive oxygen species, the molecular mechanism and biological consequence remain unclear. We investigated the structural process of S-nitrosylation of protein-tyrosine phosphatase 1B (PTP1B). We treated PTP1B with various NO donors, including S-nitrosothiol reagents and compound-releasing NO radicals, to produce site-specific Cys S-nitrosylation identified using advanced mass spectrometry (MS) techniques. Quantitative MS showed that the active site Cys-215 was the primary residue susceptible to S-nitrosylation. The crystal structure of NO donor-reacted PTP1B at 2.6 A resolution revealed that the S-NO state at Cys-215 had no discernible irreversibly oxidized forms, whereas other Cys residues remained in their free thiol states. We further demonstrated that S-nitrosylation of the Cys-215 residue protected PTP1B from subsequent H(2)O(2)-induced irreversible oxidation. Increasing the level of cellular NO by pretreating cells with an NO donor or by activating ectopically expressed NO synthase inhibited reactive oxygen species-induced irreversible oxidation of endogenous PTP1B. These findings suggest that S-nitrosylation might prevent PTPs from permanent inactivation caused by oxidative stress.
-===Crystal structure of the S-nitrosylated Cys215 of PTP1B===
+Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation.,Chen YY, Chu HM, Pan KT, Teng CH, Wang DL, Wang AH, Khoo KH, Meng TC J Biol Chem. 2008 Dec 12;283(50):35265-72. Epub 2008 Oct 7. PMID:18840608<ref>PMID:18840608</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3eu0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18840608}}, adds the Publication Abstract to the page
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18840608 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18840608}}
+__TOC__
+</StructureSection>
-==About this Structure==
-EU0 is a 1 chain structure of 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=3EU0 OCA].
-==Reference==
-Cysteine S-nitrosylation protects protein tyrosine phosphatase 1B against oxidation-induced permanent inactivation., Chen YY, Chu HM, Pan KT, Teng CH, Wang DL, Wang AH, Khoo KH, Meng TC, J Biol Chem. 2008 Oct 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18840608 18840608]
 [[Category: Homo sapiens]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Chen, Y Y.]]
+[[Category: Chen YY]]
-[[Category: Chu, H M.]]
+[[Category: Chu HM]]
-[[Category: Khoo, K H.]]
+[[Category: Khoo KH]]
-[[Category: Meng, T C.]]
+[[Category: Meng TC]]
-[[Category: Pan, K T.]]
+[[Category: Pan KT]]
-[[Category: Wang, A H.J.]]
+[[Category: Wang AHJ]]
-[[Category: Wang, D L.]]
+[[Category: Wang DL]]
-[[Category: Acetylation]]
-[[Category: Endoplasmic reticulum]]
-[[Category: Hydrolase]]
-[[Category: Membrane]]
-[[Category: Oxidation]]
-[[Category: Phosphoprotein]]
-[[Category: Polymorphism]]
-[[Category: Protein phosphatase]]
-[[Category: S-nitrosylated protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 24 11:02:57 2008''