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| <StructureSection load='1s3b' size='340' side='right'caption='[[1s3b]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='1s3b' size='340' side='right'caption='[[1s3b]], [[Resolution|resolution]] 1.65Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1s3b]] 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=1S3B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S3B FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1s3b]] 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=1S3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S3B FirstGlance]. <br> |
| </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=RMA:N-[(1S)-2,3-DIHYDRO-1H-INDEN-1-YL]-N-METHYL-N-PROP-2-YNYLAMINE'>RMA</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s2q|1s2q]], [[1s2y|1s2y]], [[1s3e|1s3e]]</div></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=RMA:N-[(1S)-2,3-DIHYDRO-1H-INDEN-1-YL]-N-METHYL-N-PROP-2-YNYLAMINE'>RMA</scene></td></tr> |
| <tr id='gene'><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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3b OCA], [https://pdbe.org/1s3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s3b RCSB], [https://www.ebi.ac.uk/pdbsum/1s3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s3b ProSAT]</span></td></tr> |
| <tr id='activity'><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>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1s3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3b OCA], [http://pdbe.org/1s3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s3b RCSB], [http://www.ebi.ac.uk/pdbsum/1s3b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s3b ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://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. | | [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=1s3b 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=1s3b ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Monoamine oxidase B (MAO B) is an outer mitochondrial membrane enzyme that catalyzes the oxidation of arylalkylamine neurotransmitters. The crystal structures of MAO B in complex with four of the N-propargylaminoindan class of MAO covalent inhibitors (rasagiline, N-propargyl-1(S)-aminoindan, 6-hydroxy-N-propargyl-1(R)-aminoindan, and N-methyl-N-propargyl-1(R)-aminoindan) have been determined at a resolution of better than 2.1 A. Rasagiline, 6-hydroxy-N-propargyl-1(R)-aminoindan, and N-methyl-N-propargyl-1(R)-aminoindan adopt essentially the same conformation with the extended propargyl chain covalently bound to the flavin and the indan ring located in the rear of the substrate cavity. N-Propargyl-1(S)-aminoindan binds with the indan ring in a flipped conformation with respect to the other inhibitors, which causes a slight movement of the Tyr326 side chain. Four ordered water molecules are an integral part of the active site and establish H-bond interactions to the inhibitor atoms. These structural studies may guide future drug design to improve selectivity and efficacy by introducing appropriate substituents on the rasagiline molecular scaffold.
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| Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class.,Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A J Med Chem. 2004 Mar 25;47(7):1767-74. PMID:15027868<ref>PMID:15027868</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1s3b" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Monoamine oxidase|Monoamine oxidase]] | | *[[Monoamine oxidase|Monoamine oxidase]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Monoamine oxidase]]
| | [[Category: Binda C]] |
| [[Category: Binda, C]] | | [[Category: Edmondson DE]] |
| [[Category: Edmondson, D E]] | | [[Category: Herzig Y]] |
| [[Category: Herzig, Y]] | | [[Category: Hubalek F]] |
| [[Category: Hubalek, F]] | | [[Category: Li M]] |
| [[Category: Li, M]] | | [[Category: Mattevi A]] |
| [[Category: Mattevi, A]] | | [[Category: Sterling J]] |
| [[Category: Sterling, J]] | |
| [[Category: Enantioselectivity]]
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| [[Category: Flavin]]
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| [[Category: Human monoamine oxidase]]
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| [[Category: Inhibitor binding]]
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| [[Category: Oxidoreductase]]
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| [[Category: Rasagiline]]
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