Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit.
A synthetic peptide corresponding to the transmembrane segment M2 (residues 236-267) of the alpha-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 alpha-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.
Pashkov
V S
VS
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Maslennikov
I V
IV
Tchikin
L D
LD
Efremov
R G
RG
Ivanov
V T
VT
Arseniev
A S
AS
D000595:Amino Acid Sequence; D000818:Animals; D002725:Chloroform / Q000737:chemistry; D007473:Ion Channels / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D000432:Methanol / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry*; D012984:Software; D014101:Torpedo / Q000378:metabolism
D007473:Ion Channels; D011978:Receptors, Nicotinic; D002725:Chloroform; D000432:Methanol