3po7: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==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 [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3PO7 FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=ZON:1-(1,2-BENZOXAZOL-3-YL)METHANESULFONAMIDE'>ZON</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=3po7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3po7 OCA], [https://pdbe.org/3po7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3po7 RCSB], [https://www.ebi.ac.uk/pdbsum/3po7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3po7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AOFB_HUMAN AOFB_HUMAN] Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine. | |||
<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> | |||
<div class="pdbe-citations 3po7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Monoamine oxidase|Monoamine oxidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Aldeco | [[Category: Aldeco M]] | ||
[[Category: Binda | [[Category: Binda C]] | ||
[[Category: Edmondson | [[Category: Edmondson DE]] | ||
[[Category: Mattevi | [[Category: Mattevi A]] | ||
Latest revision as of 20:07, 1 November 2023
Human monoamine oxidase B in complex with zonisamideHuman monoamine oxidase B in complex with zonisamide
Structural highlights
FunctionAOFB_HUMAN Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||