Modeling of Human Monoamine Oxidase A: From Low Resolution Threading Models to Accurate Comparative Models Based on Crystal Structures

Nadia Léonard, Christophe Lambert, Eric Depiereux, Johan Wouters

Résultats de recherche: Contribution à un journal/une revueArticle

Résumé

The recently published crystal structure of monoamine oxidase (MAO) B was a major breakthrough for structural and functional understanding of flavin containing amine oxidases: it opens a new era of research and provides new opportunities to those interested in the biochemistry and pharmacology of those important drug targets. In particular, it allowed accurate modeling of human MAO A, both proteins sharing over 70% sequence identity. In the present contribution, we summarize the efforts made in order to obtain structural information on the human MAO A, including sequence analysis, secondary structure predictions, and preliminary models obtained by fold recognition and comparative modeling based on proteins sharing low sequence identity.

langue originaleAnglais
Pages (de - à)47-61
Nombre de pages15
journalNeurotoxicology
Volume25
Numéro de publication1-2
Les DOIs
étatPublié - 1 janv. 2004

Empreinte digitale

Monoamine Oxidase
Crystal structure
Biochemistry
Sequence Analysis
Proteins
Pharmacology
Research
Pharmaceutical Preparations
human monoamine oxidase A

Citer ceci

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Modeling of Human Monoamine Oxidase A : From Low Resolution Threading Models to Accurate Comparative Models Based on Crystal Structures. / Léonard, Nadia; Lambert, Christophe; Depiereux, Eric; Wouters, Johan.

Dans: Neurotoxicology, Vol 25, Numéro 1-2, 01.01.2004, p. 47-61.

Résultats de recherche: Contribution à un journal/une revueArticle

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T1 - Modeling of Human Monoamine Oxidase A

T2 - From Low Resolution Threading Models to Accurate Comparative Models Based on Crystal Structures

AU - Léonard, Nadia

AU - Lambert, Christophe

AU - Depiereux, Eric

AU - Wouters, Johan

PY - 2004/1/1

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