Abstract:
:Structure-function studies have identified key functional motifs in the acetylcholine receptor, including residues that contribute to the ion channel and to the ligand-binding sites. Little is known, however, about determinants of channel gating kinetics. To identify structural correlates of gating, we examined the structural basis of the fetal-to-adult decrease in channel open time conferred by the presence of the epsilon subunit in place of the gamma subunit. By constructing chimeras composed of segments of the epsilon and gamma subunits, we show that the main determinant of this kinetic change is a 30 residue segment of a predicted amphipathic helix located between transmembrane domains M3 and M4. Further subdividing the amphipathic helix revealed that either multiple residues or its overall conformation confers this regulation of channel kinetics. We also show that L440 and M442, conserved residues within M4 of the gamma subunit, contribute to long duration openings characteristic of the fetal receptor.
journal_name
Neuronjournal_title
Neuronauthors
Bouzat C,Bren N,Sine SMdoi
10.1016/0896-6273(94)90424-3subject
Has Abstractpub_date
1994-12-01 00:00:00pages
1395-402issue
6eissn
0896-6273issn
1097-4199pii
0896-6273(94)90424-3journal_volume
13pub_type
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