1s3e: Difference between revisions

Revision as of 03:07, 29 July 2008

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File:1s3e.png

Template:STRUCTURE 1s3e

Crystal structure of MAOB in complex with 6-hydroxy-N-propargyl-1(R)-aminoindanCrystal structure of MAOB in complex with 6-hydroxy-N-propargyl-1(R)-aminoindan

Template:ABSTRACT PUBMED 15027868

About this StructureAbout this Structure

1S3E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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 {{STRUCTURE_1s3e|  PDB=1s3e  |  SCENE=  }}
-'''Crystal structure of MAOB in complex with 6-hydroxy-N-propargyl-1(R)-aminoindan'''
+===Crystal structure of MAOB in complex with 6-hydroxy-N-propargyl-1(R)-aminoindan===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15027868}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15027868 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15027868}}
 ==About this Structure==
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 [[Category: Inhibitor binding]]
 [[Category: Rasagiline]]
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