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

• Published in: FEBS letters Vol. 412; no. 3; pp. 573 - 577
• Main Authors: Perbandt, M, Wilson, J.C, Eschenburg, S, Mancheva, I, Aleksiev, B, Genov, N, Willingmann, P, Weber, W, Singh, T.P, Betzel, Ch
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 04.08.1997
• Subjects: Amino Acid Sequence; Animals; Crystallography, X-Ray; Dimerization; Evolution, Molecular; Molecular Sequence Data; Neurotoxins - antagonists & inhibitors; Neurotoxins - chemistry; Neurotoxins - toxicity; Phosphodiesterase Inhibitors - chemistry; Phosphodiesterase Inhibitors - pharmacology; Phospholipases A - antagonists & inhibitors; Phospholipases A - chemistry; Phospholipases A - toxicity; Phospholipases A2; PLA 2-complex; PLA2-complex; Protein Folding; Sequence Homology, Amino Acid; Synchrotron radiation; Viper Venoms - antagonists & inhibitors; Viper Venoms - chemistry; Viper Venoms - toxicity; Vipoxin; X-ray structure; Vipoxin; PLA 2-complex; X-ray structure; Synchrotron radiation

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 A 2 (PLA 2) and a non-toxic protein inhibitor. The structure is of genetic interest due to the high degree of sequ...