Association of beta-agonists with corresponding beta 2- and beta 1-adrenergic pentapeptide sequences.
Int J Pept Protein Res
; 41(5): 467-75, 1993 May.
Article
em En
| MEDLINE
| ID: mdl-8100557
ABSTRACT
Synthesized beta 1- and beta 2-pentapeptide sequences corresponding to published adrenoceptor transmembrane activation site subtypes were investigated in vitro for selectivity in association for drug ligands of known selectivity. Both nuclear magnetic resonance spectroscopy and molecular mechanics demonstrated that structural differences among the corresponding pentapeptide activation-site sequences can explain agonist selectivity. Results suggest the agonists bind across the activation site loop on the second transmembrane alpha-helix by dipole/dipole interactions between a ligand and the peptide. Since electrostatic interactions within the membrane may determine the rate of intercellular ion flux, agonist association across the activation site sequence could thereby decrease electrostatic resistance to positive ion flux into the cell. Interactions between the peptides and the ligands may provide insight into the structures and mechanisms involved in association of ligands for the identical sequences on the beta-adrenoreceptors.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Fragmentos de Peptídeos
/
Receptores Adrenérgicos beta
/
Agonistas Adrenérgicos beta
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Revista:
Int J Pept Protein Res
Ano de publicação:
1993
Tipo de documento:
Article