Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved

被引：265

作者：

Serrano, SMT

Maroun, RC

机构：

[1] Inst Butantan, CEPID, CAT, Lab Especial Toxinol Aplicada, BR-05503900 Sao Paulo, Brazil

[2] Inst Pasteur, Unite Bioinformat Struct, Paris, France

来源：

TOXICON | 2005年 / 45卷 / 08期

关键词：

snake venom serine proteinases; blood clotting; platelet-aggregation; kinin-release; protein-C activation; factor V activation; molecular recognition; molecular modeling; 3D structure-activity relationships;

D O I：

10.1016/j.toxicon.2005.02.020

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Snake venom glands synthesize a variety of serine protemases capable of affecting the haemostatic system. They act on macromolecular substrates of the coagulation, fibrinolytic, and kallikrein-kinin systems, and on platelets to cause an imbalance of the haemostatic system of the prey. In this review we describe their biochemical/biophysical characteristics, biological activities as well as aspects of their evolution and structure-activity relationship. (c) 2005 Elsevier Ltd. All rights reserved.

引用

收藏

页码：1115 / 1132

页数：18

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