An allosteric link connecting the lipid-protein interface to the gating of the nicotinic acetylcholine receptor.

ABSTRACT: The mechanisms underlying lipid-sensing by membrane proteins is of considerable biological importance. A unifying mechanistic question is how a change in structure at the lipid-protein interface is translated through the transmembrane domain to influence structures critical to protein function. Gating of the nicotinic acetylcholine receptor (nAChR) is sensitive to its lipid environment. To understand how changes at the lipid-protein interface influence gating, we examined how a mutation at position 418 on the lipid-facing surface of the outer most M4 transmembrane α-helix alters the energetic couplings between M4 and the remainder of the transmembrane domain. Human muscle nAChR is sensitive to mutations at position 418, with the Cys-to-Trp mutation resulting in a 16-fold potentiation in fu

SUBMITTER: Domville JA 

PROVIDER: S-EPMC5832824 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature