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

M Perbandt, Julie C. Wilson, S Eschenburg, I Mancheva, B Aleksiev, N Genov, P Willingmann, W Weber, T.P Singh, Ch Betzel

Research output: Contribution to journalArticlepeer-review


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 of phospholipases and contradicts the assumptions made in earlier studies. The modulation of PLA2 activity is of great pharmacological interest, and the present structure will be a model for structure-based drug design.
Original languageEnglish
Pages (from-to)573-577
Number of pages5
JournalFEBS Letters
Issue number3
Publication statusPublished - 4 Aug 1997


  • X-ray structure;
  • Synchrotron radiation;
  • Vipoxin;
  • PLA2-complex

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