Crystallization of Human Monoamine Oxidase B.
Crystal structure
Detergent
MAO B
Membrane protein
Monoamine oxidase B
Zwittergent 3–12
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
28
9
2022
pubmed:
29
9
2022
medline:
1
10
2022
Statut:
ppublish
Résumé
The interest in monoamine oxidases A and B (MAO A and B) is due to their central role in regulating the balance of neurotransmitters, both in the central nervous system and in peripheral organs. As validated drug targets for depression and Parkinson's disease, the elucidation of their crystal structures was an essential step to guide drug design investigations. The development of the heterologous expression system of MAO B in Pichia pastoris and the identification of the detergent, buffer, and precipitant conditions allowed to determine the first crystal structure of human MAO B in 2002. A detailed protocol to obtain reproducible MAO B crystals is described.
Identifiants
pubmed: 36169859
doi: 10.1007/978-1-0716-2643-6_9
doi:
Substances chimiques
Detergents
0
Monoamine Oxidase
EC 1.4.3.4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
115-122Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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