Structural and dynamic studies of the gamma-M4 trans-membrane domain of the nicotinic acetylcholine receptor.

Abstract:

:A structural characterization of a synthetic peptide corresponding to the fourth transmembrane domain (M4-TMD) of the gamma-subunit of the nicotinic acetylcholine receptor from Torpedo californica has been undertaken. Solid-state NMR and CD spectroscopy studies indicate that upon reconstitution into lipid vesicles or magnetically aligned lipid bilayers, the synthetic M4-TMD adopts a linear alpha-helical conformation with the helix aligned within 15 degrees of the membrane normal. Furthermore, analysis of the motional averaging of anisotropic interactions present in the solid-state NMR spectra of the reconstituted peptide, indicate that the dynamics of the peptide within the bilayer are highly sensitive to the phase adopted by the lipid bilayer, providing an insight into how the interaction of lipids with this domain may play a important role in the modulation of this receptor by its lipid environment.

journal_name

Mol Membr Biol

authors

Williamson PT,Zandomeneghi G,Barrantes FJ,Watts A,Meier BH

doi

10.1080/09687860500370653

subject

Has Abstract

pub_date

2005-11-01 00:00:00

pages

485-96

issue

6

eissn

0968-7688

issn

1464-5203

pii

W285662N81032837

journal_volume

22

pub_type

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