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

FEBS Letters

Willingmann, P¹  Perbandt, M⁶  Singh, T.P³  Wilson, J.C⁵  Mancheva, I²  Genov, N⁴  Betzel, Ch¹  Weber, W¹  Eschenburg, S¹  Aleksiev, B² 

[1] Institute of Physiological Chemistry, UKE, c/o DESY, Notkestr. 85, 22603 Hamburg, Germany;University of Chemical Technology and Metalurgy, Sofia 1040, Bulgaria;Department of Biophysics, All India Institute of Medical Sciences, New Delhi-1103 029, India;Institute of Organic Chemistry, Bulgarian Academy of Science, Sofia 1040, Bulgaria;Department of Chemistry, University of York, York Y01 5DD, UK;Institute of Biochemistry, Free University of Berlin, Thielallee 63, 14195 Berlin, Germany

关键词: X-ray structure;    Synchrotron radiation;    Vipoxin;    PLA2-complex;   

DOI  :  10.1016/S0014-5793(97)00853-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown