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A residue in the middle of the M2‐M3 loop of the β 4 subunit specifically affects gating of neuronal nicotinic receptors
Author(s) -
Rovira José Carlos,
Ballesta Juan José,
Vicente-Agulló Francisco,
Campos-Caro Antonio,
Criado Manuel,
Sala Francisco,
Sala Salvador
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00889-8
Subject(s) - gating , protein subunit , cys loop receptors , nicotinic agonist , chemistry , receptor , loop (graph theory) , biophysics , residue (chemistry) , acetylcholine receptor , biochemistry , neuroscience , nicotinic acetylcholine receptor , biology , mathematics , combinatorics , gene
An aspartate residue in the M2‐M3 loop of neuronal nicotinic receptor α 7 subunits is a major determinant of the channel functional response. This residue is conserved in most β 4 subunits, e.g. human and rat, but not in others, e.g. bovine. We have used these differences to examine the mechanism by which this residue alters the functional properties of α 3 β 4 receptors. Having ruled out an effect on the macroscopic binding ability of the agonist, the level of receptor expression, or the single channel conductance, the results suggest that receptors lacking that residue have a deficient coupling between binding and gating.