Biotinylation of substituted cysteines in the nicotinic acetylcholine receptor reveals distinct binding modes for alpha-bungarotoxin and erabutoxin a.
Spura A, Riel RU, Freedman ND, Agrawal S, Seto C, Hawrot E.
Spura A, et al. Among authors: freedman nd.
J Biol Chem. 2000 Jul 21;275(29):22452-60. doi: 10.1074/jbc.M001283200.
J Biol Chem. 2000.
PMID: 10791957
Free article.
Although previous results indicate that alpha-subunit residues Trp(187), Val(188), Phe(189), Tyr(190), and Pro(194) of the mouse nicotinic acetylcholine receptor are solvent-accessible and are in a position to contribute to the alpha-bungarotoxin (alpha-Bgtx) binding site (Spura, …
Although previous results indicate that alpha-subunit residues Trp(187), Val(188), Phe(189), Tyr(190), and Pro(194) of the mouse nicotinic a …