This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2bk3

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:13, 16 May 2018

Human Monoamine Oxidase B in complex with Farnesol

Structural highlights

2bk3 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1gos, 1h8r, 1oj9, 1oja, 1ojb, 1ojc, 1ojd, 1s2q, 1s2y, 1s3b, 1s3e, 2bk4, 2bk5
Activity:	Monoamine oxidase, with EC number 1.4.3.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Several reversible inhibitors selective for human monoamine oxidase B (MAO B) that do not inhibit MAO A have been described in the literature. The following compounds: 8-(3-chlorostyryl)caffeine, 1,4-diphenyl-2-butene, and trans,trans-farnesol are shown to inhibit competitively human, horse, rat, and mouse MAO B with K(i) values in the low micromolar range but are without effect on either bovine or sheep MAO B or human MAO A. In contrast, the reversible competitive inhibitor isatin binds to all known MAO B and MAO A with similar affinities. Sequence alignments and the crystal structures of human MAO B in complex with 1,4-diphenyl-2-butene or with trans,trans-farnesol provide molecular insights into these specificities. These inhibitors span the substrate and entrance cavities with the side chain of Ile-199 rotated out of its normal conformation suggesting that Ile-199 is gating the substrate cavity. Ile-199 is conserved in all known MAO B sequences except bovine MAO B, which has Phe in this position (the sequence of sheep MAO B is unknown). Phe is conserved in the analogous position in MAO A sequences. The human MAO B I199F mutant protein of MAO B binds to isatin (K(i) = 3 microM) but not to the three inhibitors listed above. The crystal structure of this mutant demonstrates that the side chain of Phe-199 interferes with the binding of those compounds. This suggests that the Ile-199 "gate" is a determinant for the specificity of these MAO B inhibitors and provides a molecular basis for the development of MAO B-specific reversible inhibitors without interference with MAO A function in neurotransmitter metabolism.

Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors.,Hubalek F, Binda C, Khalil A, Li M, Mattevi A, Castagnoli N, Edmondson DE J Biol Chem. 2005 Apr 22;280(16):15761-6. Epub 2005 Feb 14. PMID:15710600^[1]

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

References

↑ Hubalek F, Binda C, Khalil A, Li M, Mattevi A, Castagnoli N, Edmondson DE. Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors. J Biol Chem. 2005 Apr 22;280(16):15761-6. Epub 2005 Feb 14. PMID:15710600 doi:10.1074/jbc.M500949200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bk3"

@@ Line 1: / Line 1: @@
-==HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH FARNESOL==
+==Human Monoamine Oxidase B in complex with Farnesol==
 <StructureSection load='2bk3' size='340' side='right' caption='[[2bk3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gos|1gos]], [[1h8r|1h8r]], [[1oj9|1oj9]], [[1oja|1oja]], [[1ojb|1ojb]], [[1ojc|1ojc]], [[1ojd|1ojd]], [[1s2q|1s2q]], [[1s2y|1s2y]], [[1s3b|1s3b]], [[1s3e|1s3e]], [[2bk4|2bk4]], [[2bk5|2bk5]]</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bk3 OCA], [http://pdbe.org/2bk3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bk3 RCSB], [http://www.ebi.ac.uk/pdbsum/2bk3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bk3 OCA], [http://pdbe.org/2bk3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bk3 RCSB], [http://www.ebi.ac.uk/pdbsum/2bk3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bk3 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/2bk3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/2bk3_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 39: / Line 40: @@
 [[Category: Edmondson, D E]]
 [[Category: Mattevi, A]]
+[[Category: Acetylation]]
 [[Category: Fad]]
 [[Category: Fad-containing amine oxidase]]

2bk3

From Proteopedia

Revision as of 06:13, 16 May 2018

Human Monoamine Oxidase B in complex with Farnesol

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox