1AOK

VIPOXIN COMPLEX

Summary for 1AOK

• Entry DOI: 10.2210/pdb1aok/pdb
• Descriptor: VIPOXIN COMPLEX, ACETATE ION, ... (4 entities in total)
• Functional Keywords: phospholipase, hydrolase, vipoxin, pla2-activity, snake-venom
• Biological source: Vipera ammodytes meridionalis; More
• Cellular location: Secreted: P04084 P14420
• Total number of polymer chains: 2
• Total formula weight: 27555.92

Authors

Perbandt, M.,Wilson, J.C.,Eschenburg, S.,Betzel, C. (deposition date: 1997-07-07, release date: 1998-01-21, Last modification date: 2024-10-30)

Primary citation

Perbandt, M.,Wilson, J.C.,Eschenburg, S.,Mancheva, I.,Aleksiev, B.,Genov, N.,Willingmann, P.,Weber, W.,Singh, T.P.,Betzel, C.
Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution.
FEBS Lett., 412:573-577, 1997

PubMed Abstract: 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.

PubMed: 9276469
DOI: 10.1016/S0014-5793(97)00853-3

Experimental method

X-RAY DIFFRACTION (2 Å)