Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.06.11.145466v1?rss=1 Authors: Epstein, M., Maxwell, S., Piggot, T. J., Beeson, D., Bermudez, I., Biggin, P. C. Abstract: Muscle nicotinic acetylcholine receptors are a class of heteropentameric ligand-gated cation channels with constituent subunits adopting a fixed stoichiometric arrangement. The specific amino acid residues that govern subunit ordering are however, only partially understood. By integrating all-atom molecular dynamics simulations, bioinformatics, two-electrode voltage clamp electrophysiology and 125I--bungarotoxin assays of chimeric nAChR subunits, we identify residues across the extracellular, transmembrane and extended M4 helix of the {delta} subunit that make structural signatures that contribute to intransigent assembly rules. Furthermore, functional differences observed in 2{delta}2{beta} receptors can be rationalized by changes in dynamical behavior that manifest themselves at the agonist binding site. Copy rights belong to original authors. Visit the link for more info