Amino acids of the alpha1B-adrenergic receptor involved in agonist binding: differences in docking catecholamines to receptor subtypes.

Détails

ID Serval
serval:BIB_2DF8CBDE8971
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Amino acids of the alpha1B-adrenergic receptor involved in agonist binding: differences in docking catecholamines to receptor subtypes.
Périodique
FEBS Letters
Auteur(s)
Cavalli A., Fanelli F., Taddei C., De Benedetti P.G., Cotecchia S.
ISSN
0014-5793 (Print)
ISSN-L
0014-5793
Statut éditorial
Publié
Date de publication
1996
Volume
399
Numéro
1-2
Pages
9-13
Langue
anglais
Résumé
Site-directed mutagenesis and molecular dynamics analysis of the 3-D model of the alpha1B-adrenergic receptor (AR) were combined to identify the molecular determinants of the receptor involved in catecholamine binding. Our results indicate that the three conserved serines in the fifth transmembrane domain (TMD) of the alpha1B-AR play a distinct role in catecholamine binding versus receptor activation. In addition to the amino acids D125 in TMDIII and S207 in TMDV directly involved in ligand binding, our findings identify a large number of polar residues playing an important role in the activation process of the alpha1B-AR thus providing new insights into the structure/function relationship of G protein-coupled receptors.
Mots-clé
Adrenergic alpha-1 Receptor Agonists, Adrenergic alpha-Agonists/pharmacology, Amino Acids/chemistry, Amino Acids/genetics, Animals, COS Cells, Cricetinae, Epinephrine/metabolism, Mutagenesis, Site-Directed, Protein Binding, Receptors, Adrenergic, alpha-1/chemistry, Receptors, Adrenergic, alpha-1/genetics
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 11:05
Dernière modification de la notice
20/08/2019 13:12
Données d'usage