Nicotinic acetylcholine receptors are ligand-gated ion channels responsible for neurotransmitter-mediated signal transduction at synapses. Binding of neurotransmitter molecules to subunit interfaces in the N-terminal extracellular domain induces structural rearrangements of the membrane-spanning domain permitting the influx of cations.

Molecular simulation methods are currently being used to probe how conformational changes might propagate from the ligand-binding site to the pore domain and result in channel gating.

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