A molecular modelling study of the interaction of noradrenaline with the beta 2-adrenergic receptor.
A model of the beta 2-adrenergic receptor binding site is built from the primary structure of the receptor, experimental evidence for key binding residues and analogy with a homologous protein of partially determined structure. It is suggested that residues Trp-109, Thr-110 and Asp-113 are involved in ligand binding. Noradrenaline is successfully docked into this model, and the results of an INDO molecular orbital calculation on the complex indicate that a charge transfer interaction between Trp-109 and noradrenaline is possible.
Mitchell
T J
TJ
Department of Chemistry, University of Surrey, Guildford, U.K.
Tute
M S
MS
Webb
G A
GA
D000595:Amino Acid Sequence; D001665:Binding Sites; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009638:Norepinephrine / Q000378:metabolism*; D011487:Protein Conformation; D011943:Receptors, Adrenergic, beta / Q000378:metabolism*; D012984:Software
D011943:Receptors, Adrenergic, beta; D009638:Norepinephrine