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.
Amino acids of the α1B-adrenergic receptor involved in agonist binding: further differences in docking catecholamines to receptor subtypes / A., Cavalli; Fanelli, Francesca; C., Taddei; P. G., DE BENEDETTI; S., Cotecchia. - In: FEBS LETTERS. - ISSN 0014-5793. - ELETTRONICO. - 399(1996), pp. 9-13.
Data di pubblicazione: | 1996 |
Titolo: | Amino acids of the α1B-adrenergic receptor involved in agonist binding: further differences in docking catecholamines to receptor subtypes |
Autore/i: | A., Cavalli; Fanelli, Francesca; C., Taddei; P. G., DE BENEDETTI; S., Cotecchia |
Autore/i UNIMORE: | |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1016/S0014-5793(96)01286-0 |
Rivista: | |
Volume: | 399 |
Pagina iniziale: | 9 |
Pagina finale: | 13 |
Codice identificativo ISI: | WOS:A1996VY75900002 |
Codice identificativo Scopus: | 2-s2.0-0030577241 |
Codice identificativo Pubmed: | 8980109 |
Citazione: | Amino acids of the α1B-adrenergic receptor involved in agonist binding: further differences in docking catecholamines to receptor subtypes / A., Cavalli; Fanelli, Francesca; C., Taddei; P. G., DE BENEDETTI; S., Cotecchia. - In: FEBS LETTERS. - ISSN 0014-5793. - ELETTRONICO. - 399(1996), pp. 9-13. |
Tipologia | Articolo su rivista |
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