Snake venom disintegrins:: evolution of structure and function

被引：224

作者：

Calvete, JJ

Marcinkiewicz, C

Monleón, D

Esteve, V

Celda, B

Juárez, P

Sanz, L

机构：

[1] CSIC, Inst Biomed Valencia, E-46010 Valencia, Spain

[2] Temple Univ, Ctr Neurovirol & Canc Biol, Dept Biol, Philadelphia, PA 19122 USA

[3] Univ Valencia, Dept Quim Fis, E-46100 Burjassot, Valencia, Spain

[4] Univ Valencia, Serv Cent Soporte Invest Expt, E-46100 Burjassot, Valencia, Spain

来源：

TOXICON | 2005年 / 45卷 / 08期

关键词：

snake venom proteins; disintegrins; integrin antagonists; structure-function correlations; evolution of protein structure; disulfide bond engineering;

D O I：

10.1016/j.toxicon.2005.02.024

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Disintegrins represent a family of polypeptides present in the venoms of various vipers that selectively block the function of integrin receptors. Here, we review our current view and hypothesis on the emergence and the structural and functional diversification of disintegrins by accelerated evolution and the selective loss of disulfide bonds of duplicated genes. Research on disintegrins is relevant for understanding the biology of viper venom toxins, but also provides information on new structural determinants involved in integrin recognition that may be useful in basic and clinical research. The role of the composition, conformation, and dynamics of the integrin inhibitory loop acting in concert with the C-terminal tail in determining the selective inhibition of integrin receptors is discussed. (c) 2005 Elsevier Ltd. All rights reserved.

引用

页码：1063 / 1074

页数：12

共 69 条

[1] Structural requirements of MLD-containing disintegrins for functional interaction with α4β1 and α9β1 integrins [J].