2vz2

From Proteopedia

(Difference between revisions)

Revision as of 15:38, 13 December 2023

Human MAO B in complex with mofegiline

Structural highlights

2vz2 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Milczek EM, Bonivento D, Binda C, Mattevi A, McDonald IA, Edmondson DE. Structural and Mechanistic Studies of Mofegiline Inhibition of Recombinant Human Monoamine Oxidase B ( parallel). J Med Chem. 2008 Dec 2. PMID:19053775 doi:10.1021/jm8011867

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Homo sapiens | Large Structures | Bonivento D | Mattevi A

@@ Line 3: / Line 3: @@
 <StructureSection load='2vz2' size='340' side='right'caption='[[2vz2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vz2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
+<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>
-</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>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c67|2c67]], [[1oja|1oja]], [[2v5z|2v5z]], [[1s3e|1s3e]], [[2c73|2c73]], [[1ojb|1ojb]], [[2v60|2v60]], [[2byb|2byb]], [[2vrm|2vrm]], [[2c65|2c65]], [[2c64|2c64]], [[1oj9|1oj9]], [[1ojd|1ojd]], [[1s3b|1s3b]], [[2c66|2c66]], [[2bk4|2bk4]], [[2bk5|2bk5]], [[2c70|2c70]], [[1h8r|1h8r]], [[2c75|2c75]], [[2bk3|2bk3]], [[2v61|2v61]], [[2c72|2c72]], [[1s2y|1s2y]], [[1gos|1gos]], [[1s2q|1s2q]], [[2c76|2c76]], [[2vrl|2vrl]], [[1ojc|1ojc]]</div></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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=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.
+[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]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Monoamine oxidase]]
+[[Category: Bonivento D]]
-[[Category: Bonivento, D]]
+[[Category: Mattevi A]]
-[[Category: Mattevi, A]]
-[[Category: Acetylation]]
-[[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]]

2vz2

From Proteopedia

Revision as of 15:38, 13 December 2023

Human MAO B in complex with mofegiline

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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