2vz2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:33, 6 November 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2vz2.png|left|200px]]
 
-
<!--
+
==Human MAO B in complex with mofegiline==
-
The line below this paragraph, containing "STRUCTURE_2vz2", creates the "Structure Box" on the page.
+
<StructureSection load='2vz2' size='340' side='right'caption='[[2vz2]], [[Resolution|resolution]] 2.30&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'>[[2vz2]] 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=2VZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VZ2 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]] 2.3&#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=MFG:(1Z)-4-(4-FLUOROPHENYL)-2-METHYLIDENEBUTAN-1-IMINE'>MFG</scene></td></tr>
-
{{STRUCTURE_2vz2| PDB=2vz2 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vz2 OCA], [https://pdbe.org/2vz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vz2 RCSB], [https://www.ebi.ac.uk/pdbsum/2vz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vz2 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/vz/2vz2_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2vz2 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Mechanistic and structural studies have been carried out to investigate the molecular basis for the irreversible inhibition of human MAO-B by mofegiline. Competitive inhibition with substrate shows an apparent K(i) of 28 nM. Irreversible inhibition of MAO-B occurs with a 1:1 molar stoichiometry with no observable catalytic turnover. The absorption spectral properties of mofegiline inhibited MAO-B show features (lambda(max) approximately 450 nm) unlike those of traditional flavin N(5) or C(4a) adducts. Visible and near-UV circular dichroism spectra of the mofegiline-MAO-B adduct shows a negative peak at 340 nm with an intensity similar to that of N(5) flavocyanine adducts. The X-ray crystal structure of the mofegiline-MAO-B adduct shows a covalent bond between the flavin cofactor N(5) with the distal allylamine carbon atom as well as the absence of the fluorine atom. A mechanism to explain these structural and spectral data is proposed.
-
===HUMAN MAO B IN COMPLEX WITH MOFEGILINE===
+
Structural and Mechanistic Studies of Mofegiline Inhibition of Recombinant Human Monoamine Oxidase B ( parallel).,Milczek EM, Bonivento D, Binda C, Mattevi A, McDonald IA, Edmondson DE J Med Chem. 2008 Dec 2. PMID:19053775<ref>PMID:19053775</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2vz2" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_19053775}}, adds the Publication Abstract to the page
+
*[[Monoamine oxidase|Monoamine oxidase]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 19053775 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_19053775}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
2VZ2 is a 2 chains structure of 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=2VZ2 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:19053775</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Bonivento, D.]]
+
[[Category: Large Structures]]
-
[[Category: Mattevi, A.]]
+
[[Category: Bonivento D]]
-
[[Category: Acetylation]]
+
[[Category: Mattevi A]]
-
[[Category: Fad]]
+
-
[[Category: Flavin]]
+
-
[[Category: Flavoprotein]]
+
-
[[Category: Human monoamine oxidase]]
+
-
[[Category: Inhibitor binding]]
+
-
[[Category: Membrane]]
+
-
[[Category: Mitochondrion]]
+
-
[[Category: Mitochondrion outer membrane]]
+
-
[[Category: Mofegiline]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Transmembrane]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 22 20:20:55 2009''
+

Current revision

Human MAO B in complex with mofegiline

PDB ID 2vz2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vz2"
Personal tools