Structure of a Lys49 phospholipase A2 homologue isolated from the venom of Bothrops nummifer (jumping viper)

被引：38
作者：
de Azevedo, WF
Ward, RJ
Gutiérrez, JM
Arni, RK
机构：
[1] UNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
[2] Univ Sao Paulo, FMRP, Dept Biochem, Ribeirao Preto, Brazil
[3] Univ Costa Rica, Inst Clodomiro Picado, San Jose, Costa Rica
来源：
TOXICON | 1999年 / 37卷 / 02期
基金：
巴西圣保罗研究基金会;
关键词：
D O I：
10.1016/S0041-0101(98)00189-5
中图分类号：
R9 [药学];
学科分类号：
1007 ;
摘要：
Lys49-Phospholipase A(2) (Lys49-PLA(2)) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity, We have solved the structure of myotoxin-I, a Lys49-PLA(2) homologue isolated from the venom of Bothrops nummifer (jumping viper) at 2.4 Angstrom resolution using molecular replacement techniques. The final model has been refined to a final R-factor of 18.4% (R-free = 23.2%), and shows excellent geometry, The myotoxin-I from Bothrops nummifer is dimeric in the crystalline state as has been observed for other Lys49-PLA(2) homologues. In addition, a continuous electron density in the active site and substrate binding channel could be successfully modeled as a fatty-acid molecule. (C) 1999 Elsevier Science Ltd, All rights reserved.
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收藏
页码：371 / 384
页数：14
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