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- W2004236906 abstract "The lipid-protein interface is an important domain of the acetylcholine receptor (AChR) that has recently garnered increasing relevance. Several studies have made significant advances toward determining the structure and dynamics of the lipid-exposed domains of the AChR. However, there is still a need to identify and gain insight into the mechanism through which lipid-protein interactions regulate AChR function and dynamics. In this study, we extend the Fourier Transform coupled Tryptophan Scanning Mutagenesis (FT-TrpScanM) approach to monitor the conformational changes experienced by the δM3 and δM4 transmembrane domains of the Torpedo californica AChR, and to identify which lipid-exposed positions on these domains are potentially linked to the regulation of ion channel kinetics. The perturbations produced by periodic tryptohan substitutions along the δM3 and δM4 transmembrane domains were characterized by two-electrode voltage clamp and 125I-labeled α-bungarotoxin binding assays. The periodicity profiles and Fourier Transform spectra of these domains revealed a thinner-elongated helical structure for the closed-channel state and a thicker-shrunken helical structure for the open-channel state. The difference in oscillation patterns between the closed- and open-channel states shows a substantial conformational change along these domains as a consequence of channel activation. These results support the recently proposed spring model for the αM3 transmembrane domain of the Mus musculus AChR. Furthermore, the present data demonstrates that the lipid-protein interface of the AChR plays an important role in the propagation of the conformational wave needed for channel gating. Supported by NIH Grants 2RO1GM56371-12 and 2U54NS43011." @default.
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- W2004236906 date "2010-01-01" @default.
- W2004236906 modified "2023-09-26" @default.
- W2004236906 title "Fourier Transform Coupled Tryptophan Scanning Mutagenesis of the Lipid Exposed DM3 And DM4 Transmembrane Domains of the Torpedo Californica Acetylcholine Receptor" @default.
- W2004236906 doi "https://doi.org/10.1016/j.bpj.2009.12.712" @default.
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