2x0y: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2x0y.png|left|200px]]
-<!--
+==Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds==
-The line below this paragraph, containing "STRUCTURE_2x0y", creates the "Structure Box" on the page.
+<StructureSection load='2x0y' size='340' side='right'caption='[[2x0y]], [[Resolution|resolution]] 2.25&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'>[[2x0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X0Y 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]] 2.25&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=X0T:7-[(2S)-2,3-DIHYDROXYPROPYL]-1,3-DIMETHYL-3,7-DIHYDRO-1H-PURINE-2,6-DIONE'>X0T</scene></td></tr>
-{{STRUCTURE_2x0y|  PDB=2x0y  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0y OCA], [https://pdbe.org/2x0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x0y RCSB], [https://www.ebi.ac.uk/pdbsum/2x0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x0y ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
+== 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/x0/2x0y_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=2x0y ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+O-GlcNAcylation is an essential posttranslational modification in metazoa. Modulation of O-GlcNAc levels with small molecule inhibitors of O-GlcNAc hydrolase (OGA) is a useful strategy to probe the role of this modification in a range of cellular processes. Here we report the discovery of novel, low molecular weight and drug-like O-GlcNAcase inhibitor scaffolds by high-throughput screening. Kinetic and X-ray crystallographic analyses of the binding modes with human/bacterial O-GlcNAcases identify some of these as competitive inhibitors. Comparative kinetic experiments with the mechanistically related human lysosomal hexosaminidases reveal that three of the inhibitor scaffolds show selectivity towards human OGA. These scaffolds provide attractive starting points for the development of non-carbohydrate, drug-like OGA inhibitors.
-===SCREENING-BASED DISCOVERY OF DRUG-LIKE O-GLCNACASE INHIBITOR SCAFFOLDS===
+Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds.,Dorfmueller HC, van Aalten DM FEBS Lett. 2010 Feb 19;584(4):694-700. Epub 2009 Dec 16. PMID:20026047<ref>PMID:20026047</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_20026047}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2x0y" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 20026047 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_20026047}}
-==About this Structure==
-[[2x0y]] is a 2 chain structure of [[Beta-Hexosaminidase]] with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0Y OCA].
 ==See Also==
-*[[Beta-Hexosaminidase]]
+*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
+*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
-==Reference==
+*[[O-GlcNAcase|O-GlcNAcase]]
-<ref group="xtra">PMID:020026047</ref><references group="xtra"/>
+== References ==
-[[Category: Beta-N-acetylhexosaminidase]]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Clostridium perfringens]]
-[[Category: Aalten, D M.F Van.]]
+[[Category: Large Structures]]
-[[Category: Dorfmueller, H C.]]
+[[Category: Dorfmueller HC]]
+[[Category: Van Aalten DMF]]