Theillet Francois-Xavier, Kalmar Lajos, Tompa Peter, Han Kyou-Hoon, Selenko Philipp, Dunker A Keith, Daughdrill Gary W, Uversky Vladimir N
In-cell NMR Spectroscopy; Leibniz Institute of Molecular Pharmacology (FMP Berlin); Berlin, Germany.
VIB Department of Structural Biology; Vrije Universiteit Brussel; Brussels, Belgium.
Intrinsically Disord Proteins. 2013 Apr 1;1(1):e24360. doi: 10.4161/idp.24360. eCollection 2013 Jan-Dec.
A significant fraction of every proteome is occupied by biologically active proteins that do not form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) have essential biological functions and are characterized by extensive structural plasticity. Such structural and functional behavior is encoded in the amino acid sequences of IDPs/IDPRs, which are enriched in disorder-promoting residues and depleted in order-promoting residues. In fact, amino acid residues can be arranged according to their disorder-promoting tendency to form an alphabet of intrinsic disorder that defines the structural complexity and diversity of IDPs/IDPRs. This review is the first in a series of publications dedicated to the roles that different amino acid residues play in defining the phenomenon of protein intrinsic disorder. We start with proline because data suggests that of the 20 common amino acid residues, this one is the most disorder-promoting.
每个蛋白质组中相当一部分是由不形成独特三维结构的生物活性蛋白质占据的。这些内在无序蛋白质（IDP）和内在无序蛋白区域（IDPR）具有重要的生物学功能，其特征是具有广泛的结构可塑性。这种结构和功能行为由IDP/IDPR的氨基酸序列编码，这些序列富含促进无序的残基而缺乏促进有序的残基。事实上，氨基酸残基可以根据其促进无序的倾向进行排列，形成一个内在无序字母表，它定义了IDP/IDPR的结构复杂性和多样性。本综述是一系列致力于探讨不同氨基酸残基在定义蛋白质内在无序现象中所起作用的出版物中的第一篇。我们从脯氨酸开始，因为数据表明，在20种常见氨基酸残基中，脯氨酸是促进无序作用最强的。
