Dynamic multivalent interactions of intrinsically disordered proteins

被引：41

作者：

Weng, Jingwei ^{[1
]}

Wang, Wenning ^{[1
]}

机构：

[1] Fudan Univ, Multiscale Res Inst Complex Syst, Dept Chem, Shanghai, Peoples R China

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2020年 / 62卷

基金：

中国国家自然科学基金;

关键词：

STRUCTURAL BASIS; FUZZY COMPLEXES; FG-NUCLEOPORINS; BINDING; RECOGNITION; SPECIFICITY; BIOLOGY;

D O I：

10.1016/j.sbi.2019.11.001

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：

Protein-protein interactions involving intrinsically disordered proteins (IDPs) usually display dynamic and multivalent features. Recent experimental data revealed myriad functional roles of the dynamic multivalent interaction (DMI) of IDPs. However, characterization of DMI remains a challenge due to its complex and promiscuous nature. Recent studies start showing that understanding the mechanistic role of DMI relies on combined use of various techniques and construction of microscopic models in elucidating the binding thermodynamics and kinetics.

引用

页码：9 / 13

页数：5

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