Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor α‐subunit

FEBS Letters

Tchikin, Leonid D¹  Maslennikov, Innokenty V¹  Arseniev, Alexander S¹  Efremov, Roman G¹  Pashkov, Vladimir S¹  Ivanov, Vadim T¹ 

[1] Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya, Moscow 117871, Russia

关键词: Nicotinic acetylcholine receptor;    Membrane domain;    NMR;    Conformational analysis;    nAChR;    nicotinic acetylcholine receptor;    DQF-COSY;    double-quantum-filtered COSY;    NOE;    nuclear Overhauser effect;    MHP;    molecular hydrophobicity potential;    TM;    transmembrane;   

DOI  :  10.1016/S0014-5793(99)01023-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A synthetic peptide corresponding to the transmembrane segment M2 (residues 236–267) of the α-subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by two dimensional ¹H-NMR spectroscopy in a chloroform-methanol (1:1) mixture containing 0.1 M LiClO₄. Reconstruction of the spatial structure of M2 from the NMR data resulted in an α-helix formed by residues 241–263. Distribution of the molecular hydrophobicity potential on the helix surface is very similar to that in five-helix bundles of proteins with a known three dimensional structure: two hydrophilic bands located on the opposite helix sides separated by strong hydrophobic zones.

【 授权许可】

Unknown