Your browser version may not work well with NCBI's Web applications. More information here...
1: J Mol Biol. 1993 May 20;231(2):498-500.Click here to read Links

Crystallization and preliminary X-ray analysis of vipoxin, a complex between a toxic phospholipase A2 and its natural polypeptide inhibitor.

Betzel C, Visanji M, Wilson KS, Genov N, Mancheva I, Aleksiev B, Singh T.

European Molecular Biology Laboratory, DESY, Hamburg, Germany.

The toxin vipoxin, which is a complex between a basic toxic phospholipase A2 and an acidic non-toxic protein inhibitor, is found in the venom of the Bulgarian viper (Vipera ammodytes ammodytes), the most toxic snake in Europe. The two polypeptide chains each consist of 122 residues and are highly homologous (62%). The vipoxin complex is the first reported example of a high degree of structural homology between an enzyme and its natural inhibitor. The present crystals diffract in the X-ray beam to 1.8 A resolution. The space group is P2(1)2(1)2(1). The cell dimensions are a = 45.80 A, b = 55.36 A and c = 107.69 A. Native data to a resolution of 2.8 A have been recorded.

PMID: 8510159 [PubMed - indexed for MEDLINE]