A ring of uncharged polar amino acids as a component of channel constriction in the nicotinic acetylcholine receptor

Keiji Imoto, Takashi Konno, Junichi Nakai, Feng Wang, Masayoshi Mishina, Shosaku Numa

研究成果: Article査読

101 被引用数 (Scopus)

抄録

The channel pore of the nicotinic acetylcholine receptor (AChR) has been investigated by analysing single-channel conductances of systematically mutatedTorpedo receptors expressed in Xenopus oocytes. The mutations mainly alter the size and polarity of uncharged polar amino acid residues of the acetylcholine receptor subunits positioned between the cytoplasmic ring and the extracellular ring. From the results obtained, we conclude that a ring of uncharged polar residues comprising threonine 244 of the α-subunit (αT244), βS250, γT253 and δS258 (referred to as the central ring) and the anionic intermediate ring, which are adjacent to each other in the assumed α-helical configuration of the M2-containing transmembrane segment, together form a narrow channel constriction of short length, located close to the cytoplasmic side of the membrane. Our results also suggest that individual subunits, particularly the γ-subunit, are asymmetrically positioned at the channel constriction.

本文言語English
ページ(範囲)193-200
ページ数8
ジャーナルFEBS Letters
289
2
DOI
出版ステータスPublished - 1991 9 9
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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