Article
Molecular mechanisms of ligand-receptor interactions in transmembrane domain V of the alpha2A-adrenoceptor.
British journal of pharmacology - 1 Sept 2003
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
Abstract excerpt
1. The structural determinants of catechol hydroxyl interactions with adrenergic receptors were examined using 12 alpha2-adrenergic agonists and a panel of mutated human alpha2A-adrenoceptors. The alpha2ASer201 mutant had a Cys --> Ser201 (position 5.43) amino-acid substitution, and alpha2ASer201Cys200 and alpha2ASer201Cys204 had Ser --> Cys200 (5.42) and Ser --> Cys204 (5.46) substitutions, respectively, in...
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