2xfn: Difference between revisions

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-{{Seed}}
-[[Image:2xfn.jpg|left|200px]]
-<!--
+==Human monoamine oxidase B in complex with 2-(2-benzofuranyl)-2- imidazoline==
-The line below this paragraph, containing "STRUCTURE_2xfn", creates the "Structure Box" on the page.
+<StructureSection load='2xfn' size='340' side='right'caption='[[2xfn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2xfn]] 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=2XFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XFN FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C15:N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE'>C15</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene></td></tr>
-{{STRUCTURE_2xfn|  PDB=2xfn  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfn OCA], [https://pdbe.org/2xfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfn RCSB], [https://www.ebi.ac.uk/pdbsum/2xfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfn 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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/2xfn_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2xfn ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Crystallographic and biochemical studies have been employed to identify the binding site and mechanism for potentiation of imidazoline-binding in human monoamine oxidase B (MAO B). 2-(2-Benzofuranyl)-2-imidazoline (2-BFI) inhibits recombinant human MAO B with a Ki of 8.3+/-0.6 muM whereas tranylcypromine-inhibited MAO B binds 2-BFI with a Kd of 9+/-2 nM, representing an increase in binding energy Delta(DeltaG) of -3.9 kcal/mol. Crystal structures show the imidazoline ligand bound in a site that is distinct from the substrate-binding cavity. Contributions to account for the increase in binding affinity upon tranylcypromine inhibition include a conformational change in the side chain of Gln206 and a "closed conformation" of the side chain of Ile199, forming a hydrophobic "sandwich" with the side chain of Ile316 on each face of the benzofuran ring of 2-BFI. Data with the Ile199Ala mutant of human MAO B and failure to observe a similar binding potentiation with rat MAO B, where Ile316 is replaced with a Val residue, support an allosteric mechanism where the increased binding affinity of 2-BFI results from a cooperative increase in H-bond strength through formation of a more hydrophobic milieu. These insights should prove valuable in the design of high affinity and specific reversible MAO B inhibitors.
-===HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2-BENZOFURANYL) -2-IMIDAZOLINE===
+Potentiation of ligand binding through cooperative effects in monoamine oxidase B.,Bonivento D, Milczek EM, McDonald GR, Binda C, Holt A, Edmondson DE, Mattevi A J Biol Chem. 2010 Sep 20. PMID:20855894<ref>PMID:20855894</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2xfn" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20855894}}, adds the Publication Abstract to the page
+*[[Monoamine oxidase|Monoamine oxidase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20855894 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20855894}}
+__TOC__
+</StructureSection>
-==About this Structure==
-XFN is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFN OCA].
-==Reference==
-<ref group="xtra">PMID:20855894</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Monoamine oxidase]]
+[[Category: Large Structures]]
-[[Category: Binda, C.]]
+[[Category: Binda C]]
-[[Category: Bonivento, D.]]
+[[Category: Bonivento D]]
-[[Category: Edmondson, D E.]]
+[[Category: Edmondson DE]]
-[[Category: Holt, A.]]
+[[Category: Holt A]]
-[[Category: Mattevi, A.]]
+[[Category: Mattevi A]]
-[[Category: Mcdonald, G R.]]
+[[Category: McDonald GR]]
-[[Category: Milczek, E M.]]
+[[Category: Milczek EM]]
-[[Category: Flavoprotein]]
-[[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct  6 06:03:01 2010''