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

Author:

Domville Jaimee A.,Baenziger John E.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Reference57 articles.

1. Lee, A. G. How lipids affect the activities of integral membrane proteins. Biochim Biophys Acta 1666, 62–87 (2004).

2. Epstein, M. & Racker, E. Reconstitution of carbamylcholine-dependent sodium ion flux and desensitization of the acetylcholine receptor from Torpedo californica. J Biol Chem 253, 6660–2 (1978).

3. Heidmann, T., Sobel, A., Popot, J. L. & Changeux, J. P. Reconstitution of a functional acetylcholine receptor. Conservation of the conformational and allosteric transitions and recovery of the permeability response; role of lipids. Eur J Biochem 110, 35–55 (1980).

4. Fong, T. M. & McNamee, M. G. Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes. Biochemistry 26, 3871–80 (1987).

5. Criado, M., Eibl, H. & Barrantes, F. J. Functional properties of the acetylcholine receptor incorporated in model lipid membranes. Differential effects of chain length and head group of phospholipids on receptor affinity states and receptor-mediated ion translocation. J Biol Chem 259, 9188–98 (1984).

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