Relationships between chemical structure and affinity for acetylcholine receptors

Nonsynaptic chemical transmission through nicotinic acetylcholine receptors.

This review attempts to organize the different aspects of nicotinic transmission in the context of nonsynaptic interactions. Nicotinic acetylcholine receptors (nAChRs) dominantly operate in the nonsynaptic mode in the central nervous system despite their ligand-gated ion-channel nature, which would otherwise be better suited for fast synaptic transmission. This fast form of nonsynaptic transmis...

Nonsynaptic Chemical Transmission Through Nicotinic Acetylcholine Receptors

Structure and activation of muscarinic acetylcholine receptors.

A homology model of the M(1) muscarinic acetylcholine receptor, based on the X-ray structure of bovine rhodopsin, has been used to interpret the results of scanning and point mutagenesis studies on the receptor's transmembrane (TM) domain. Potential intramolecular interactions that are important for the stability of the protein fold have been identified. The residues contributing to the binding...

α9α10 acetylcholine receptors: structure and functions

The α9 and α10 nicotinic acetylcholine receptor (nAChR) subunits assemble as pentameric complexes with a central ligand-gated cation-selective pore. However, these subunits do not assemble with other nAChR subunits. The general topology of each subunit is similar to that of other ligand-gated, Cys-loop ion channels. Although the sequence and genomic organization of the α9 and α10 subunits deter...

High-affinity binding of [3H]acetylcholine to muscarinic cholinergic receptors.

High-affinity binding of [3H]acetylcholine to muscarinic cholinergic sites in rat CNS and peripheral tissues was measured in the presence of cytisin, which occupies nicotinic cholinergic receptors. The muscarinic sites were characterized with regard to binding kinetics, pharmacology, anatomical distribution, and regulation by guanyl nucleotides. These binding sites have characteristics of high-...