3po7
From Proteopedia
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| - | [[ | + | ==Human monoamine oxidase B in complex with zonisamide== | 
| + | <StructureSection load='3po7' size='340' side='right' caption='[[3po7]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3po7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PO7 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=ZON:1-(1,2-BENZOXAZOL-3-YL)METHANESULFONAMIDE'>ZON</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAOB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=3po7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3po7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3po7 RCSB], [http://www.ebi.ac.uk/pdbsum/3po7 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The binding of zonisamide to purified, recombinant monoamine oxidases (MAOs) has been investigated. It is a competitive inhibitor of human MAO B (K(i) = 3.1 +/- 0.3 muM), of rat MAO B (K(i) = 2.9 +/- 0.5 muM), and of zebrafish MAO (K(i) = 30.8 +/- 5.3 muM). No inhibition is observed with purified human or rat MAO A. The 1.8 A structure of the MAO B complex demonstrates that it binds within the substrate cavity. | ||
| - | + | Interactions of Monoamine Oxidases with the Antiepileptic Drug Zonisamide: Specificity of Inhibition and Structure of the Human Monoamine Oxidase B Complex.,Binda C, Aldeco M, Mattevi A, Edmondson DE J Med Chem. 2010 Dec 22. PMID:21175212<ref>PMID:21175212</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Human]] | |
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| - | [[Category:  | + | |
| [[Category: Monoamine oxidase]] | [[Category: Monoamine oxidase]] | ||
| [[Category: Aldeco, M.]] | [[Category: Aldeco, M.]] | ||
Revision as of 13:11, 18 May 2014
Human monoamine oxidase B in complex with zonisamide
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