A1 Refereed original research article in a scientific journal
Conserved structural, pharmacological and functional properties among the three human and five zebrafish alpha(2)-adrenoceptors
Authors: Ruuskanen JO, Laurila J, Xhaard H, Rantanen VV, Vuoriluoto K, Wurster S, Marjamaki A, Vainio M, Johnson MS, Scheinin M
Publisher: NATURE PUBLISHING GROUP
Publication year: 2005
Journal:: British Journal of Pharmacology
Journal name in source: BRITISH JOURNAL OF PHARMACOLOGY
Journal acronym: BRIT J PHARMACOL
Volume: 144
Issue: 2
First page : 165
Last page: 177
Number of pages: 13
ISSN: 0007-1188
DOI: https://doi.org/10.1038/sj.bjp.0706057
Abstract
4 The alpha(2A) orthologues and the zebrafish alpha(2D) duplicates clustered as close pairs, but the relationships between the orthologues of alpha(2B) and alpha(2C) were not clearly defined. Applied to the ligands, our clustering methods segregated the ligands based on their chemical structures and functional properties. As the ligand binding pockets formed by the transmembrane helices show only minor differences among the alpha(2)-adrenoceptors, we suggest that the second extracellular loop - where significant sequence variability is located - might contribute significantly to the observed affinity differences.
4 The alpha(2A) orthologues and the zebrafish alpha(2D) duplicates clustered as close pairs, but the relationships between the orthologues of alpha(2B) and alpha(2C) were not clearly defined. Applied to the ligands, our clustering methods segregated the ligands based on their chemical structures and functional properties. As the ligand binding pockets formed by the transmembrane helices show only minor differences among the alpha(2)-adrenoceptors, we suggest that the second extracellular loop - where significant sequence variability is located - might contribute significantly to the observed affinity differences.
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