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AChR structure: a new twist in the story

https://doi.org/10.1016/0166-2236(85)90002-5Get rights and content

Abstract

The amino acid sequence for all four subunits of the acetylcholine receptor (AChR) channel has now been determined by molecular biological techniques1. As this sequence information became available, a number of laboratories proposed structures for the membrane-spanning portions of the channel. These proposals fell into two classes with very different views of what ions passing through the pore would see. Models in the first class1–3, pictured a pore that would be uncharged and lined with hydrophilic side chains, whereas the second class of models4,5 predicted a charge lined pore with alternating regions where positive and negative charges predominate. Recent reports of work in two laboratories provide evidence that the second class of models is correct6–8.

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