1gos
From Proteopedia
(Difference between revisions)
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<StructureSection load='1gos' size='340' side='right'caption='[[1gos]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1gos' size='340' side='right'caption='[[1gos]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1gos]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1gos]] 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=1GOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GOS FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id=' | + | <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=NYP:N-[(E)-METHYL](PHENYL)-N-[(E)-2-PROPENYLIDENE]METHANAMINIUM'>NYP</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=1gos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gos OCA], [https://pdbe.org/1gos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gos RCSB], [https://www.ebi.ac.uk/pdbsum/1gos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gos ProSAT]</span></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=1gos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gos OCA], [https://pdbe.org/1gos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gos RCSB], [https://www.ebi.ac.uk/pdbsum/1gos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gos ProSAT]</span></td></tr> | ||
</table> | </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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gos ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gos ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Monoamine oxidase B (MAO B) is a mitochondrial outermembrane flavoenzyme that is a well-known target for antidepressant and neuroprotective drugs. We determined the structure of the human enzyme to 3 A resolution. The enzyme binds to the membrane through a C-terminal transmembrane helix and apolar loops located at various positions in the sequence. The electron density shows that pargyline, an analog of the clinically used MAO B inhibitor, deprenyl, binds covalently to the flavin N5 atom. The active site of MAO B consists of a 420 A(3)-hydrophobic substrate cavity interconnected to an entrance cavity of 290 A(3). The recognition site for the substrate amino group is an aromatic cage formed by Tyr 398 and Tyr 435. The structure provides a framework for probing the catalytic mechanism, understanding the differences between the B- and A-monoamine oxidase isoforms and designing specific inhibitors. | ||
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| - | Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders.,Binda C, Newton-Vinson P, Hubalek F, Edmondson DE, Mattevi A Nat Struct Biol. 2002 Jan;9(1):22-6. PMID:11753429<ref>PMID:11753429</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1gos" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Monoamine oxidase|Monoamine oxidase]] | *[[Monoamine oxidase|Monoamine oxidase]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Binda C]] | |
| - | [[Category: Binda | + | [[Category: Edmondson DE]] |
| - | [[Category: Edmondson | + | [[Category: Hubalek F]] |
| - | [[Category: Hubalek | + | [[Category: Mattevi A]] |
| - | [[Category: Mattevi | + | [[Category: Newton-Vinson P]] |
| - | [[Category: Newton-Vinson | + | |
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| - | + | ||
Current revision
Human Monoamine Oxidase B
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