2qep: Difference between revisions

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[[Image:2qep.gif|left|200px]]


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==Crystal structure of the D1 domain of PTPRN2 (IA2beta)==
The line below this paragraph, containing "STRUCTURE_2qep", creates the "Structure Box" on the page.
<StructureSection load='2qep' size='340' side='right'caption='[[2qep]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2qep]] 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=2QEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QEP 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]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
{{STRUCTURE_2qep|  PDB=2qep  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qep OCA], [https://pdbe.org/2qep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qep RCSB], [https://www.ebi.ac.uk/pdbsum/2qep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qep ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTPR2_HUMAN PTPR2_HUMAN] Implicated in development of nervous system and pancreatic endocrine cells.<ref>PMID:8878534</ref> <ref>PMID:8798755</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/qe/2qep_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=2qep ConSurf].
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== 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 the D1 domain of PTPRN2 (IA2beta)'''
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 2qep" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2QEP is a [[Single protein]] 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=2QEP OCA].
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Alfano I]]
[[Category: Alfano, I.]]
[[Category: Arrowsmith CH]]
[[Category: Arrowsmith, C H.]]
[[Category: Barr A]]
[[Category: Barr, A.]]
[[Category: Berridge G]]
[[Category: Berridge, G.]]
[[Category: Bunkoczi G]]
[[Category: Bunkoczi, G.]]
[[Category: Burgess-Brown N]]
[[Category: Burgess-Brown, N.]]
[[Category: Das S]]
[[Category: Das, S.]]
[[Category: Edwards A]]
[[Category: Delft, F von.]]
[[Category: Fedorov O]]
[[Category: Edwards, A.]]
[[Category: King O]]
[[Category: Fedorov, O.]]
[[Category: Knapp S]]
[[Category: King, O.]]
[[Category: Niesen F]]
[[Category: Knapp, S.]]
[[Category: Pike ACW]]
[[Category: Niesen, F.]]
[[Category: Salah E]]
[[Category: Pike, A C.W.]]
[[Category: Savitsky P]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Sundstrom M]]
[[Category: Salah, E.]]
[[Category: Ugochukwu E]]
[[Category: Savitsky, P.]]
[[Category: Watt S]]
[[Category: Sundstrom, M.]]
[[Category: Weigelt J]]
[[Category: Ugochukwu, E.]]
[[Category: Von Delft F]]
[[Category: Watt, S.]]
[[Category: Weigelt, J.]]
[[Category: Autoantigen]]
[[Category: Ia-2 beta]]
[[Category: Phogrin]]
[[Category: Ptprn2]]
[[Category: Ptprp]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
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