An extracellular RRR motif flanking the M1 transmembrane domain governs the biogenesis of homomeric neuronal nicotinic acetylcholine receptors

Charged amino acid motifs flanking each

Charged amino acid motifs flanking each extreme of the αM4 transmembrane domain are involved in assembly and cell-surface targeting of the muscle nicotinic acetylcholine receptor

✍ A.M. Roccamo; F.J. Barrantes 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 382 KB

## Abstract The αM4 transmembrane domain of the nicotinic acetylcholine receptor (AChR) is flanked by two basic amino acids (His^408^ and Arg^429^) located at its cytoplasmic‐ and extracellular‐facing extremes, respectively, at the level of the phospholipid polar head regions of the postsynaptic me