A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Conserved structural, pharmacological and functional properties among the three human and five zebrafish alpha(2)-adrenoceptors
Tekijät: Ruuskanen JO, Laurila J, Xhaard H, Rantanen VV, Vuoriluoto K, Wurster S, Marjamaki A, Vainio M, Johnson MS, Scheinin M
Kustantaja: NATURE PUBLISHING GROUP
Julkaisuvuosi: 2005
Lehti:: British Journal of Pharmacology
Tietokannassa oleva lehden nimi: BRITISH JOURNAL OF PHARMACOLOGY
Lehden akronyymi: BRIT J PHARMACOL
Vuosikerta: 144
Numero: 2
Aloitussivu: 165
Lopetussivu: 177
Sivujen määrä: 13
ISSN: 0007-1188
DOI: https://doi.org/10.1038/sj.bjp.0706057
Tiivistelmä
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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