1aok
VIPOXIN COMPLEX
Structural highlights
FunctionPA2HA_VIPAE Heterodimer: postsynaptic neurotoxin.[1] Monomer: Acidic phospholipase A2 homolog that is non-toxic.[2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedVipoxin 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. Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution.,Perbandt M, Wilson JC, Eschenburg S, Mancheva I, Aleksiev B, Genov N, Willingmann P, Weber W, Singh TP, Betzel C FEBS Lett. 1997 Aug 4;412(3):573-7. PMID:9276469[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||
