Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution.

@article{Perbandt1997CrystalSO,
  title={Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution.},
  author={Marcus Perbandt and Jennifer C. Wilson and Susanne Eschenburg and I. N. Mancheva and Boris Aleksiev and Nicolay C. Genov and Peter Willingmann and Wolfgang Weber and Tej Pratap Singh and Ch Betzel},
  journal={FEBS letters},
  year={1997},
  volume={412 3},
  pages={573-7}
}
Vipoxin is the main toxic component in the venom of the Bulgarian snake Vipera ammodytes meridionalis, the most toxic snake in Europe. Vipoxin is a complex between a toxic phospholipase A2 (PLA2) and a non-toxic protein inhibitor. The structure is of genetic interest due to the high degree of sequence homology (62%) between the two functionally different components. The structure shows that the formation of the complex in vipoxin is significantly different to that seen in many known structures… CONTINUE READING