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
- 8 May 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 155 (2) , 245-247
- https://doi.org/10.1016/0014-5793(82)80613-3
Abstract
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 outlinedKeywords
This publication has 6 references indexed in Scilit:
- Partial tertiary structure assignment for the acetylcholine receptor on the basis of the hydrophobicity of amino acid sequences and channel location using single group rotation theoryBiochemical and Biophysical Research Communications, 1983
- Nucleotide and deduced amino acid sequences of Torpedo californica acetylcholine receptor gamma subunit.Proceedings of the National Academy of Sciences, 1983
- Sequence banks: Searching for sequence similaritiesNature, 1983
- Primary structures of β- and δ-subunit precursors of Torpedo californica acetylcholine receptor deduced from cDNA sequencesNature, 1983
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Acetylcholine Receptor: Complex of Homologous SubunitsScience, 1980