Acetylcholine-binding protein (AChBP) from the mollusc Lymnaea stagnalis is at present the only high-resolution model for the ligand-binding domains of the ligand-gated ion channel family, which includes nicotinic acetylcholine, 5HT3, GABAA, GABAC and glycine receptors. Here we present crystal structures from remote homologs from other molluscs that will define the variabilities in the binding ...

Ionotropic GABAA and GABAC receptors play an important role in the operation of CNS and serve as targets for many neuroactive drugs. Using the homology modelling and molecular dynamics, the 3D models of the receptors were built and some aspects of ligandtarget interactions were elucidated [1,2]. To better understand the structural factors controlling the activity and selectivity of the ligands,...

The prototypic member of the acetylcholine receptor family, the muscle nicotinic receptor, is a heteromeric complex with five subunits but only two ligand-binding sites. However, some members of this receptor superfamily are homomeric, containing five seemingly identical binding sites. Whether activation actually requires binding of five agonist molecules in this situation is unclear. Such ques...

Nicotinic acetylcholine receptors are prototypes for the pharmaceutically important family of pentameric ligand-gated ion channels. Here we present atomic resolution structures of nicotine and carbamylcholine binding to AChBP, a water-soluble homolog of the ligand binding domain of nicotinic receptors and their family members, GABAA, GABAC, 5HT3 serotonin, and glycine receptors. Ligand binding ...

Polyclonal antibodies against the N terminus of the rat rho 1 subunit were generated to study the distribution of GABAc receptors in the mammalian retina. The specificity of the antibodies was tested in Western blots and transfected HEK-293 cells. No cross-reactivity with the GABAA receptor subunits alpha 1-3, beta 1-3, gamma 2, delta or with the glycine receptor subunits alpha 1 and beta could...