Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex

@article{Bourne1995AcetylcholinesteraseIB,
  title={Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex},
  author={Yves Bourne and Palmer Taylor and Pascale Marchot},
  journal={Cell},
  year={1995},
  volume={83},
  pages={503-512}
}
The crystal structure of the snake toxin fasciculin, bound to mouse acetylcholinesterase (mAChE), at 3.2 A resolution reveals a synergistic three-point anchorage consistent with the picomolar dissociation constant of the complex. Loop II of fasciculin contains a cluster of hydrophobic residues that interact with the peripheral anionic site of the enzyme and sterically occlude substrate access to the catalytic site. Loop I fits in a crevice near the lip of the gorge to maximize the surface area… CONTINUE READING

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