4p58
From Proteopedia
(Difference between revisions)
m (Protected "4p58" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | ''' | + | ==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P58 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2F6:1,3-DIMETHYL-1H,1H-3,4-BIPYRAZOLE'>2F6</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p58 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p58 RCSB], [http://www.ebi.ac.uk/pdbsum/4p58 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Catechol O-methyltransferase]] | ||
| + | [[Category: Lanier, M.]] | ||
| + | [[Category: Sam binding site]] | ||
Revision as of 06:20, 25 June 2014
Crystal structure of mouse comt bound to an inhibitor
| |||||||||||
