Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors.
作者： E. G. Peralta , A. Ashkenazi , J. W. Winslow , D. H. Smith , J. Ramachandran
DOI: 10.1002/J.1460-2075.1987.TB02733.X
关键词: Ligand (biochemistry) 、 Receptor 、 Peptide sequence 、 Muscarinic acetylcholine receptor M2 、 Cholinergic 、 Molecular biology 、 Biology 、 Acetylcholine receptor 、 Muscarinic acetylcholine receptor 、 Gene expression
摘要: To investigate the molecular basis for diversity in muscarinic cholinergic function, we have isolated genes encoding human M1 and M2 receptors (mAChR) as well two previously undiscovered mAChR subtypes, designated HM3 HM4. The amino acid sequence of each subtype reflects a structure consisting seven, highly conserved transmembrane segments large intracellular region unique to subtype, which may constitute ligand-binding effector-coupling domains respectively. Significant differences affinity ligands were detected individual subtypes produced by transfection mammalian cells. Each exhibited multiple states agonists; among affinities proportions such sites suggest capacity interact differentially with cellular apparatus. Subtype-specific mRNA expression was observed heart, pancreas neuronal cell line, indicating that regulation gene contributes differentiation activity.
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