Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit.,Pashkov VS, Maslennikov IV, Tchikin LD, Efremov RG, Ivanov VT, Arseniev AS FEBS Lett. 1999 Aug 20;457(1):117-21. PMID:10486576[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pashkov VS, Maslennikov IV, Tchikin LD, Efremov RG, Ivanov VT, Arseniev AS. Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit. FEBS Lett. 1999 Aug 20;457(1):117-21. PMID:10486576
