›› 2006, Vol. 49 ›› Issue (3): 491-496.

• 研究论文 • 上一篇    下一篇

昆虫抗冻蛋白: 规则结构适应功能

邵强,李海峰,徐存拴   

  1. 河南师范大学生命科学学院
  • 出版日期:2006-07-10 发布日期:2006-06-20

New advances on insect antifreeze proteins:Regular structure suitable for function

SHAO Qiang, LI Hai-Feng, XU Cun-Shuan   

  1. College of Life Sciences, Henan Normal University
  • Online:2006-07-10 Published:2006-06-20

摘要:

抗冻蛋白在环境温度低于体液熔点时能够结合到生物体内的冰核表面,通过限制冰核生长和抑制冰晶重结晶而保护有机体免受结冰引起的伤害。与其他生物抗冻蛋白比较,昆虫抗冻蛋白有很强的活性,结构上具有显著特征,如一级结构规律重复,超二级结构为β-螺旋,可与冰晶发生相互作用,具有TXT基序等。该文综述了近年来关于昆虫抗冻蛋白的结构以及分子生物学等方面研究的新进展,讨论了其结构与功能的关系。

关键词: 昆虫, 抗冻蛋白, β-螺旋结构, TXT基序, 表达

Abstract:

Antifreeze proteins are also defined as thermal hysteresis proteins. They are one kind of functional proteins discovered in many organisms. When the temperature is subzero, they can bind to the surface of the ice nucleations to restrict their growth so as to protect organisms from injury caused by freezing. Insect antifreeze proteins have special structures such as repeat sequences, β-helix and TXT motifs. Additionally, they have stronger antifreeze activity than antifreeze proteins of other organisms. In this article, the special properties of insect antifreeze protein are introduced in detail; new advances on their structure and molecular biology are reviewed. Meanwhile, the function of TXT motif and the relationship between structure and function are discussed.
 

Key words: Insect, antifreeze protein, β-helix, TXT motif, expression