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Beta-adrenoceptors: three-dimensional structures and binding sites for ligands Nagatomo T; Ohnuki T; Ishiguro M; Ahmed M; Nakamura TJpn J Pharmacol 2001[Sep]; 87 (1): 7-13Recent progress in analyzing the structures and functions of G-protein coupled receptors (GPCRs) including beta-adrenoceptors (beta-ARs) has been made by pharmacological, physiological and molecular biological techniques. The three-dimensional (3D) structures, interaction sites with ligands and conformational changes of these receptor subtypes due to ligand binding are now better understood by the simulation of these receptors using computer-aided molecular modeling. Based on these techniques, numbers and conformations of amino acid sequences of each subtype (beta1-, beta2- and beta3-ARs) were defined and also interaction sites or modes of interaction between ligands and beta-ARs could be analyzed three-dimensionally. In addition, simulation of 3D structures of beta-ARs by molecular modeling could clearly determine the limited size, space or pocket for fitting with ligands. These studies will give some clues for the clarification of other GPCRs. Thus, this review summarizes current findings on chemical structures of ligands, amino acid sequences, 3D structures and important amino acids of beta-AR subtypes for interacting with ligands obtained from mutagenesis, chimeric studies and molecular modeling techniques.|Amino Acid Sequence[MESH]|Binding Sites[MESH]|GTP-Binding Proteins/metabolism[MESH]|Humans[MESH]|Ligands[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Molecular Structure[MESH]|Protein Conformation[MESH]|Receptors, Adrenergic, beta/*chemistry/metabolism[MESH]|Signal Transduction[MESH]|Structure-Activity Relationship[MESH] |
