Nicotinic acetylcholine (ACh) receptors convert the binding of ACh into the opening of a cation-conducting channel. New information about the regions of the receptor most immediately involved in its function, namely the ACh-binding sites, the gate and the channel, has come from two approaches. One is the identification by labelling and by mutagenesis of residues contributing to these regions. Another is the determination of the three-dimensional structure of the receptor by electron microscopy. Although the identification of functionally relevant residues is incomplete and residues cannot yet be resolved in the three-dimensional structure, the two approaches are converging. There is still room in the gap for speculation.