Partial tertiary structure assignments for the β‐, γ‐ and δ‐ subunits of the acetylcholine receptor on the basis of the hydrophobicity of amino acid sequences and channel location using single group rotation theory

FEBS Letters

Kosower, Edward M.¹ 

[1] Department of Chemistry, Tel-Aviv University, Ramat-Aviv, Tel-Aviv 69978 Israel

关键词: Acetylcholine receptor;    Subunit β;    γ;    δ;    Tertiary structure;    Amino acid hydrophobicity;    Ion channel location;    Single group rotation;   

DOI  :  10.1016/0014-5793(82)80613-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Four transmembrane segments from each of the β-, γ- and δ-protein subunits of the acetylcholine receptor (AChR) [Nature (1983) 301, 251–255], [Proc. Natl. Acad. Sci. USA (1983) 80, 1111–1115] have been selected on the basis of single group rotation (SGR) theory [Symp. Structure and Dynamics of Nucleic Acids and Proteins (Sept. 1982) abst. pp.52–53], [Biochem. Biophys. Res. Commun. (1983) 111, 1022–1029] and the hydrophobicity of amino acid sequences. One helix from each subunit is assigned to the AChR ion channel. Criteria for the selection of ion channel elements are outlined.

【 授权许可】

Unknown