2ahs

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[[Image:2ahs.png|left|200px]]
 
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==Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta==
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The line below this paragraph, containing "STRUCTURE_2ahs", creates the "Structure Box" on the page.
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<StructureSection load='2ahs' size='340' side='right'caption='[[2ahs]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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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'>[[2ahs]] 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=2AHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AHS FirstGlance]. <br>
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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]] 2.1&#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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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{{STRUCTURE_2ahs| PDB=2ahs | 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=2ahs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahs OCA], [https://pdbe.org/2ahs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ahs RCSB], [https://www.ebi.ac.uk/pdbsum/2ahs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PTPRB_HUMAN PTPRB_HUMAN] Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin (By similarity).<ref>PMID:19116766</ref> <ref>PMID:19136612</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/ah/2ahs_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=2ahs 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 Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta===
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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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<div class="pdbe-citations 2ahs" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_016946481}}, adds the Publication Abstract to the page
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 016946481 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_016946481}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2ahs]] is a 2 chain structure 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=2AHS OCA].
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==Reference==
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<ref group="xtra">PMID:016946481</ref><ref group="xtra">PMID:019167335</ref><references group="xtra"/>
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[[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: Ball, L.]]
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[[Category: Ball L]]
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[[Category: Barr, A.]]
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[[Category: Barr A]]
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[[Category: Bray, J.]]
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[[Category: Bray J]]
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[[Category: Bunkoczi, G.]]
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[[Category: Bunkoczi G]]
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[[Category: Burgess, N.]]
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[[Category: Burgess N]]
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[[Category: Das, S.]]
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[[Category: Das S]]
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[[Category: Debreczeni, J.]]
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[[Category: Debreczeni J]]
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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: Gileadi O]]
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[[Category: Gileadi, O.]]
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[[Category: Knapp S]]
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[[Category: Knapp, S.]]
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[[Category: Sobott F]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Sundstrom M]]
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[[Category: Sobott, F.]]
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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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Current revision

Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta

PDB ID 2ahs

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