Photolabeling reveals the proximity of the alpha-neurotoxin binding site to the M2 helix of the ion channel in the nicotinic acetylcholine receptor.

@article{Machold1995PhotolabelingRT,
  title={Photolabeling reveals the proximity of the alpha-neurotoxin binding site to the M2 helix of the ion channel in the nicotinic acetylcholine receptor.},
  author={Jan Machold and Yu.N. Utkin and Dieter Kirsch and Ralph Kaufmann and V. I. Tsetlin and Ferdinand Hucho},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 16},
  pages={7282-6}
}
A photoactivatable derivative of neurotoxin II from Naja naja oxiana containing a 125I-labeled p-azidosalicylamidoethyl-1,3'-dithiopropyl label at Lys-25 forms a photo-induced cross-link with the delta subunit of the membrane-bound Torpedo californica nicotinic acetylcholine receptor (AChR). The cross-linked radioactive receptor peptide was isolated by reverse-phase HPLC after tryptic digestion of the labeled delta subunit. The sequence of this peptide, delta-(260-277), and the position of the… CONTINUE READING
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