物理化学学报 >> 2010, Vol. 26 >> Issue (08): 2061-2072.doi: 10.3866/PKU.WHXB20100644

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天然无序蛋白质: 序列-结构-功能的新关系

黄永棋, 刘志荣   

  1. 北京大学化学与分子工程学院, 北京大学理论生物学中心, 北京分子科学国家实验室, 北京 100871
  • 收稿日期:2010-02-03 修回日期:2010-04-01 发布日期:2010-07-23
  • 通讯作者: 刘志荣 E-mail:LiuZhiRong@pku.edu.cn
  • 基金资助:

    国家自然科学基金(20973016、10721403)、国家重点基础研究发展计划项目(973) (2009CB918500)和教育部留学回国人员科研启动基金资助

Intrinsically Disordered Proteins: the New

HUANG Yong-Qi, LIU Zhi-Rong   

  1. Beijing National Laboratory for Molecular Sciences, Center for Theoretical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, P. R. China
  • Received:2010-02-03 Revised:2010-04-01 Published:2010-07-23
  • Contact: LIU Zhi-Rong E-mail:LiuZhiRong@pku.edu.cn
  • Supported by:

    The project was supported by the National Natural Science Foundation of China (20973016, 10721403), National Key Basis Research Program of China (973) (2009CB918500), and Scientific Research Foundation for the Returned Overseas Chinese Scholars, Ministry of Education, China.

摘要:

天然无序蛋白质是一类新发现的蛋白质, 它们在天然条件下没有确定的三维结构, 却具有正常的生物学功能, 广泛参与信号传递、DNA转录、细胞分裂和蛋白质聚集等重要的生理与病理过程. 无序蛋白质的发现是对传统的蛋白质“序列-结构-功能”范式的挑战. 在这篇综述里, 我们首先回顾了蛋白质的传统范式以及无序蛋白质的发现过程, 然后介绍无序蛋白质在结构、序列、功能等方面的特征与相互作用, 并以分子识别过程为例, 进一步阐述目前国际上对无序蛋白质所具有优势的一些认识与观点. 我们还分析了无序蛋白质研究在生命科学和医学等领域的应用前景, 并介绍了国内在无序蛋白质领域的研究现状.

关键词: 天然无序蛋白质, 蛋白质折叠, 蛋白质相互作用, 分子识别, 蛋白质结构预测, 药物设计

Abstract:

Intrinsically disordered proteins (IDPs) are a new class of proteins which lack a unique tertiary structure under native conditions while possessing essential biological functions. They take part in various physiological processes such as signal transduction, transcription and translation regulation, and protein modification. The discovery of IDPs challenges the conventional protein “sequence-structure-function” paradigm. In this review, we first overview the history of the conventional protein paradigm and the discovery of IDPs. Then we discuss the characteristics of IDPs in terms of sequence, structure, and biological function. Taking molecular recognition processes as an example, we further introduce current opinions on the advantages of IDPs in binding. Finally, we analyze possible applications of the study of IDPs such as further understanding the protein folding mechanism, improving protein structure determination, providing new clues for protein design and new targets for drug design. The current status of IDPs study in China is also briefly presented.

Key words: Intrinsically disordered protein, Protein folding, Protein interaction, Molecular recognition

MSC2000: 

  • O641