Disorder transitions and conformational diversity cooperatively modulate biological function in proteins

被引：13

作者：

Javier Zea, Diego ^{[1
]}

Miguel Monzon, Alexander ^{[1
]}

Gonzalez, Claudia ^{[1
]}

Silvina Fornasari, Maria ^{[1
]}

Tosatto, Silvio C. E. ^{[2
]}

Parisi, Gustavo ^{[1
]}

机构：

[1] Natl Univ Quilmes, Dept Sci & Technol, Struct Bioinformat Grp, Bernal, Argentina

[2] Univ Padua, Dept Biomed Sci, Biocomp Up, I-35100 Padua, Italy

来源：

PROTEIN SCIENCE | 2016年 / 25卷 / 06期

关键词：

disorder; conformational diversity; protein function; transitions; STRUCTURAL DISORDER; INTRINSIC DISORDER; DYNAMICS; ALLOSTERY; DATABASE; ENSEMBLES; CATALYSIS;

D O I：

10.1002/pro.2931

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Structural differences between conformers sustain protein biological function. Here, we studied in a large dataset of 745 intrinsically disordered proteins, how ordered-disordered transitions modulate structural differences between conformers as derived from crystallographic data. We found that almost 50% of the proteins studied show no transitions and have low conformational diversity while the rest show transitions and a higher conformational diversity. In this last subset, 60% of the proteins become more ordered after ligand binding, while 40% more disordered. As protein conformational diversity is inherently connected with protein function our analysis suggests differences in structure-function relationships related to order-disorder transitions.

引用

页码：1138 / 1146

页数：9