Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors.

@article{Bourne2005CrystalSO,
  title={Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors.},
  author={Yves Bourne and Todd T. Talley and Scott B. Hansen and Palmer Taylor and Pascale Marchot},
  journal={The EMBO journal},
  year={2005},
  volume={24 8},
  pages={1512-22}
}
The crystal structure of the snake long alpha-neurotoxin, alpha-cobratoxin, bound to the pentameric acetylcholine-binding protein (AChBP) from Lymnaea stagnalis, was solved from good quality density maps despite a 4.2 A overall resolution. The structure unambiguously reveals the positions and orientations of all five three-fingered toxin molecules inserted at the AChBP subunit interfaces and the conformational changes associated with toxin binding. AChBP loops C and F that border the ligand… CONTINUE READING

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