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The “gating” residues Ile199 and Tyr326 in human monoamine oxidase B function in substrate and inhibitor recognition

The major structural difference between human monoamine oxidases A (MAO A) and B (MAO B) is that MAO A has a monopartite substrate cavity of ~550 Å(3) volume and MAO B contains a dipartite cavity structure with volumes of ~290 Å(3) (entrance cavity) and ~400 Å(3) (substrate cavity). Ile199 and Tyr32...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Milczek, Erika M., Binda, Claudia, Rovida, Stefano, Mattevi, Andrea, Edmondson, Dale E.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2011
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC3228903/
https://ncbi.nlm.nih.gov/pubmed/21978362
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1111/j.1742-4658.2011.08386.x
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