2p6x: Difference between revisions

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-{{Seed}}
-[[Image:2p6x.png|left|200px]]
-<!--
+==Crystal structure of human tyrosine phosphatase PTPN22==
-The line below this paragraph, containing "STRUCTURE_2p6x", creates the "Structure Box" on the page.
+<StructureSection load='2p6x' size='340' side='right'caption='[[2p6x]], [[Resolution|resolution]] 1.90&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'>[[2p6x]] is a 2 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=2P6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P6X 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]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-{{STRUCTURE_2p6x|  PDB=2p6x  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p6x OCA], [https://pdbe.org/2p6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p6x RCSB], [https://www.ebi.ac.uk/pdbsum/2p6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p6x ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/PTN22_HUMAN PTN22_HUMAN] Defects in PTPN22 are a cause of susceptibility to systemic lupus erythematosus (SLE) [MIM:[https://omim.org/entry/152700 152700]. SLE is a chronic, inflammatory and often febrile multisystemic disorder of connective tissue. It affects principally the skin, joints, kidneys and serosal membranes. It is thought to represent a failure of the regulatory mechanisms of the autoimmune system.<ref>PMID:15273934</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/PTN22_HUMAN PTN22_HUMAN] Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue. Dephosphorylates ZAP70 at its activating 'Tyr-493' residue. Dephosphorylates the immune system activator SKAP2.<ref>PMID:16461343</ref> <ref>PMID:18056643</ref> <ref>PMID:19167335</ref> <ref>PMID:21719704</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/p6/2p6x_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=2p6x ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently found in phosphatases, and this has implications for both substrate recognition and development of selective inhibitors. Structural comparison identified four diverse catalytic loop (WPD) conformations and suggested a mechanism for loop closure. Enzymatic assays revealed vast differences in PTP catalytic activity and identified PTPD1, PTPD2, and HDPTP as catalytically inert protein phosphatases. We propose a "head-to-toe" dimerization model for RPTPgamma/zeta that is distinct from the "inhibitory wedge" model and that provides a molecular basis for inhibitory regulation. This phosphatome resource gives an expanded insight into intrafamily PTP diversity, catalytic activity, substrate recognition, and autoregulatory self-association.
-===Crystal structure of human tyrosine phosphatase PTPN22===
+Large-scale structural analysis of the classical human protein tyrosine phosphatome.,Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, Alfano I, Savitsky P, Burgess-Brown NA, Muller S, Knapp S Cell. 2009 Jan 23;136(2):352-63. PMID:19167335<ref>PMID:19167335</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2p6x" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19167335}}, 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 19167335 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19167335}}
+__TOC__
+</StructureSection>
-==About this Structure==
-P6X is a 2 chains structure of sequences 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=2P6X OCA].
-==Reference==
-<ref group="xtra">PMID:19167335</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Alfano, I.]]
+[[Category: Alfano I]]
-[[Category: Arrowsmith, C H.]]
+[[Category: Arrowsmith CH]]
-[[Category: Barr, A.]]
+[[Category: Barr A]]
-[[Category: Bunkoczi, G.]]
+[[Category: Bunkoczi G]]
-[[Category: Burgess-Brown, N.]]
+[[Category: Burgess-Brown N]]
-[[Category: Delft, F von.]]
+[[Category: Edwards A]]
-[[Category: Edwards, A.]]
+[[Category: King O]]
-[[Category: King, O.]]
+[[Category: Knapp S]]
-[[Category: Knapp, S.]]
+[[Category: Papagrigoriou E]]
-[[Category: Papagrigoriou, E.]]
+[[Category: Pike ACW]]
-[[Category: Pike, A C.W.]]
+[[Category: Salah E]]
-[[Category: SGC, Structural Genomics Consortium.]]
+[[Category: Shrestha L]]
-[[Category: Salah, E.]]
+[[Category: Sundstrom M]]
-[[Category: Shrestha, L.]]
+[[Category: Turnbull A]]
-[[Category: Sundstrom, M.]]
+[[Category: Ugochukwu E]]
-[[Category: Turnbull, A.]]
+[[Category: Umeano C]]
-[[Category: Ugochukwu, E.]]
+[[Category: Uppenberg J]]
-[[Category: Umeano, C.]]
+[[Category: Weigelt J]]
-[[Category: Uppenberg, J.]]
+[[Category: Von Delft F]]
-[[Category: Weigelt, J.]]
-[[Category: Hydrolase]]
-[[Category: Lymphoid phosphatase]]
-[[Category: Lyp]]
-[[Category: Pep]]
-[[Category: Sgc]]
-[[Category: Structural genomic]]
-[[Category: Structural genomics consortium]]
-[[Category: Tyrosine phosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:29:32 2009''