2gjt

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[[Image:2gjt.png|left|200px]]
 
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==Crystal structure of the human receptor phosphatase PTPRO==
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The line below this paragraph, containing "STRUCTURE_2gjt", creates the "Structure Box" on the page.
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<StructureSection load='2gjt' size='340' side='right'caption='[[2gjt]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2gjt]] 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=2GJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GJT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#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>
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{{STRUCTURE_2gjt| PDB=2gjt | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjt OCA], [https://pdbe.org/2gjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gjt RCSB], [https://www.ebi.ac.uk/pdbsum/2gjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gjt ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/PTPRO_HUMAN PTPRO_HUMAN] Defects in PTPRO are the cause of nephrotic syndrome type 6 (NPHS6) [MIM:[https://omim.org/entry/614196 614196]. NPHS6 is a renal disease characterized clinically by proteinuria, hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure.<ref>PMID:21722858</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/PTPRO_HUMAN PTPRO_HUMAN] Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function (By similarity).<ref>PMID:19167335</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/2gjt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2gjt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of the human receptor phosphatase PTPRO===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19167335}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2gjt" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19167335 is the PubMed ID number.
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{{ABSTRACT_PUBMED_19167335}}
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==About this Structure==
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[[2gjt]] is a 2 chain structure of [[Proten tyrosine phosphatase]] and [[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=2GJT OCA].
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==See Also==
==See Also==
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*[[Proten tyrosine phosphatase]]
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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*[[Tyrosine phosphatase]]
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:019167335</ref><references group="xtra"/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C.]]
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[[Category: Arrowsmith C]]
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[[Category: Barr, A.]]
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[[Category: Barr A]]
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[[Category: Das, S.]]
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[[Category: Das S]]
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[[Category: Delft, F von.]]
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[[Category: Edwards A]]
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[[Category: Edwards, A.]]
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[[Category: Eswaran J]]
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[[Category: Eswaran, J.]]
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[[Category: Knapp S]]
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[[Category: Knapp, S.]]
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[[Category: Niesen F]]
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[[Category: Niesen, F.]]
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[[Category: Papagrigoriou E]]
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[[Category: Papagrigoriou, E.]]
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[[Category: Savitsky P]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Sundstrom M]]
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[[Category: Savitsky, P.]]
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[[Category: Turnbull A]]
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[[Category: Sundstrom, M.]]
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[[Category: Ugochukwu E]]
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[[Category: Turnbull, A.]]
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[[Category: Weigelt J]]
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[[Category: Ugochukwu, E.]]
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[[Category: Von Delft F]]
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[[Category: Weigelt, J.]]
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[[Category: Glepp1]]
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[[Category: Hydrolase]]
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[[Category: Ptpro]]
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[[Category: Ptpu2]]
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[[Category: Sgc]]
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[[Category: Structural genomic]]
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[[Category: Structural genomics consortium]]
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[[Category: Tyrosine phosphatase]]
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Current revision

Crystal structure of the human receptor phosphatase PTPRO

PDB ID 2gjt

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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