2i3u: Difference between revisions

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-[[Image:2i3u.png|left|200px]]
-{{STRUCTURE_2i3u|  PDB=2i3u  |  SCENE=  }}
+==Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors==
+<StructureSection load='2i3u' size='340' side='right'caption='[[2i3u]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2i3u]] 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=2I3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I3U FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3u OCA], [https://pdbe.org/2i3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i3u RCSB], [https://www.ebi.ac.uk/pdbsum/2i3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3u ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== 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/i3/2i3u_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=2i3u ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein tyrosine phosphatases (PTPs) play roles in many biological processes and are considered to be important targets for drug discovery. As inhibitor development has proven challenging, crystal structure-based design will be very helpful to advance inhibitor potency and selectivity. Successful application of protein crystallography to drug discovery heavily relies on high-quality crystal structures of the protein of interest complexed with pharmaceutically interesting ligands. It is very important to be able to produce protein-ligand crystals rapidly and reproducibly for as many ligands as necessary. This study details our efforts to engineer the catalytic domain of human protein tyrosine phosphatase beta (HPTPbeta-CD) with properties suitable for rapid-turnaround crystallography. Structures of apo HPTPbeta-CD and its complexes with several novel small-molecule inhibitors are presented here for the first time.
-===Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors===
+Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery.,Evdokimov AG, Pokross M, Walter R, Mekel M, Cox B, Li C, Bechard R, Genbauffe F, Andrews R, Diven C, Howard B, Rastogi V, Gray J, Maier M, Peters KG Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1435-45. Epub 2006, Nov 23. PMID:17139078<ref>PMID:17139078</ref>
-{{ABSTRACT_PUBMED_17139078}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2i3u" style="background-color:#fffaf0;"></div>
-[[2i3u]] is a 1 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=2I3U OCA].
 ==See Also==
-*[[Proten tyrosine phosphatase|Proten tyrosine phosphatase]]
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
-*[[Tyrosine phosphatase|Tyrosine phosphatase]]
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:017139078</ref><references group="xtra"/>
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Evdokimov, A G.]]
+[[Category: Evdokimov AG]]
-[[Category: Mekel, M.]]
+[[Category: Mekel M]]
-[[Category: Pokross, M E.]]
+[[Category: Pokross ME]]
-[[Category: Walter, R L.]]
+[[Category: Walter RL]]
-[[Category: Drug design]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor]]
-[[Category: Phosphatase]]
-[[Category: Protein tyrosine phosphatase]]
-[[Category: Sulfamic acid]]
-[[Category: Wpd-loop]]