2x0y: Difference between revisions
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<StructureSection load='2x0y' size='340' side='right'caption='[[2x0y]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='2x0y' size='340' side='right'caption='[[2x0y]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2x0y]] is a 2 chain structure with sequence from [ | <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> | ||
</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> | </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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j62|2j62]], [[2cbi|2cbi]], [[2jh2|2jh2]], [[2wb5|2wb5]], [[2v5c|2v5c]], [[2cbj|2cbj]], [[2vur|2vur]], [[2v5d|2v5d]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2j62|2j62]], [[2cbi|2cbi]], [[2jh2|2jh2]], [[2wb5|2wb5]], [[2v5c|2v5c]], [[2cbj|2cbj]], [[2vur|2vur]], [[2v5d|2v5d]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 34: | Line 34: | ||
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | *[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | ||
*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] | *[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] | ||
*[[O-GlcNAcase|O-GlcNAcase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:44, 13 April 2022
Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffoldsScreening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds
Structural highlights
Function[OGA_CLOP1] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedO-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.,Dorfmueller HC, van Aalten DM FEBS Lett. 2010 Feb 19;584(4):694-700. Epub 2009 Dec 16. PMID:20026047[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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