1AOK

VIPOXIN COMPLEX

1AOK の概要

• エントリーDOI: 10.2210/pdb1aok/pdb
• 分子名称: VIPOXIN COMPLEX, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: phospholipase, hydrolase, vipoxin, pla2-activity, snake-venom
• 由来する生物種: Vipera ammodytes meridionalis; 詳細
• 細胞内の位置: Secreted: P04084 P14420
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27555.92

構造登録者

Perbandt, M.,Wilson, J.C.,Eschenburg, S.,Betzel, C. (登録日: 1997-07-07, 公開日: 1998-01-21, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)