Structural highlights
Function
[ACHA_TORCA] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
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
