A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip.

Abstract excerpt

Nicotinic acetylcholine receptors are allosteric proteins that generate membrane currents by isomerizing ("gating") between resting and active conformations under the influence of neurotransmitters. Here, to explore the mechanisms that link the transmitter-binding sites (TBSs) with the distant gate, we use mutant cycle analyses to measure coupling between residue pairs, phi value analyses to sequence domain...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Binding Sites
• Share to Crystallography, X-Ray
• Share to Ion Channel Gating