Nicotinic receptor transduction zone: invariant arginine couples to multiple electron-rich residues.

ABSTRACT: Gating of the muscle-type acetylcholine receptor (AChR) channel depends on communication between the ACh-binding site and the remote ion channel. A key region for this communication is located within the structural transition zone between the ligand-binding and pore domains. Here, stemming from β-strand 10 of the binding domain, the invariant αArg209 lodges within the hydrophobic interior of the subunit and is essential for rapid and efficient channel gating. Previous charge-reversal experiments showed that the contribution of αArg209 to channel gating depends strongly on αGlu45, also within this region. Here we determine whether the contribution of αArg209 to channel gating depends on additional anionic or electron-rich residues in this region. Also, to reconcile diverging findings in the

SUBMITTER: Mukhtasimova N 

PROVIDER: S-EPMC3552258 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature