Molecular mechanisms of ligand–receptor interactions in transmembrane domain V of the α(2A)-adrenoceptor

1. The structural determinants of catechol hydroxyl interactions with adrenergic receptors were examined using 12 α(2)-adrenergic agonists and a panel of mutated human α(2A)-adrenoceptors. The α(2A)Ser201 mutant had a Cys → Ser201 (position 5.43) amino-acid substitution, and α(2A)Ser201Cys200 and α(...

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Main Authors: Peltonen, Juha M, Nyrönen, Tommi, Wurster, Siegfried, Pihlavisto, Marjo, Hoffrén, Anna-Marja, Marjamäki, Anne, Xhaard, Henri, Kanerva, Liisa, Savola, Juha-Matti, Johnson, Mark S, Scheinin, Mika
Formato: Artigo
Idioma:Inglês
Publicado em: 2003
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Papers
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1574035/
https://ncbi.nlm.nih.gov/pubmed/12970108
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/sj.bjp.0705439
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