4p58
From Proteopedia
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(New page: '''Unreleased structure''' The entry 4p58 is ON HOLD Authors: Lanier, M. Description: Crystal structure of mouse comt bound to an inhibitor) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of mouse comt bound to an inhibitor== | |
| + | <StructureSection load='4p58' size='340' side='right'caption='[[4p58]], [[Resolution|resolution]] 2.06Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4p58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P58 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]] 2.06Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2F6:1,3-DIMETHYL-1H,1H-3,4-BIPYRAZOLE'>2F6</scene></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=4p58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p58 OCA], [https://pdbe.org/4p58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p58 RCSB], [https://www.ebi.ac.uk/pdbsum/4p58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p58 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/COMT_MOUSE COMT_MOUSE] Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Catechol O-methyl transferase belongs to the diverse family of S-adenosyl-l-methionine transferases. It is a target involved in the treatment of Parkinson's disease. Here we present a fragment-based screening approach to discover noncatechol derived COMT inhibitors which bind at the SAM binding pocket. We describe the identification and characterization of a series of highly ligand efficient SAM competitive bisaryl fragments (LE = 0.33-0.58). We also present the first SAM-competitive small-molecule COMT co-complex crystal structure. | ||
| - | + | A Fragment-Based Approach to Identifying S-Adenosyl-l-methionine -Competitive Inhibitors of Catechol O-Methyl Transferase (COMT).,Lanier M, Ambrus G, Cole DC, Davenport R, Ellery J, Fosbeary R, Jennings AJ, Kadotani A, Kamada Y, Kamran R, Matsumoto SI, Mizukami A, Okubo S, Okada K, Saikatendu K, Walsh L, Wu H, Hixon MS J Med Chem. 2014 Jun 4. PMID:24847974<ref>PMID:24847974</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4p58" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Lanier M]] | ||
Current revision
Crystal structure of mouse comt bound to an inhibitor
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