Homologous mutations on different subunits cause unequal but additive effects on n-alcohol block in the nicotinic receptor pore.

doi:10.1016/S0006-3495(97)78860-X

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Article

Homologous mutations on different subunits cause unequal but additive effects on n-alcohol block in the nicotinic receptor pore.

Biophysical journal - 1 May 1997

Forman S A

Abstract excerpt

Hydrophobic antagonists of the nicotinic acetylcholine receptor inhibit channel activity by binding within the transmembrane pore formed by the second of four transmembrane domains (M2) on each of the receptor's subunits. Hydrophobic mutagenesis near the middle (10' locus) of the alpha-subunit M2...

Topics

Alcohols
Amino Acid Sequence
Animals
Ion Channel Gating
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Receptors, Nicotinic
Sequence Alignment
Xenopus

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