The Dynamic Multisite Interactions between Two Intrinsically Disordered Proteins
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- Shaowen Wu
- Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials Department of Chemistry, and Institutes of Biomedical Sciences Fudan University Shanghai 200433 China
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- Dongdong Wang
- Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials Department of Chemistry, and Institutes of Biomedical Sciences Fudan University Shanghai 200433 China
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- Jin Liu
- Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials Department of Chemistry, and Institutes of Biomedical Sciences Fudan University Shanghai 200433 China
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- Yitao Feng
- Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials Department of Chemistry, and Institutes of Biomedical Sciences Fudan University Shanghai 200433 China
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- Jingwei Weng
- Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials Department of Chemistry, and Institutes of Biomedical Sciences Fudan University Shanghai 200433 China
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- Yu Li
- King Abdullah University of Science and Technology (KAUST) Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division Thuwal 23955 Saudi Arabia
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- Xin Gao
- King Abdullah University of Science and Technology (KAUST) Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division Thuwal 23955 Saudi Arabia
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- Jianwei Liu
- Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials Department of Chemistry, and Institutes of Biomedical Sciences Fudan University Shanghai 200433 China
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- Wenning Wang
- Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials Department of Chemistry, and Institutes of Biomedical Sciences Fudan University Shanghai 200433 China
説明
<jats:title>Abstract</jats:title><jats:p>Protein interactions involving intrinsically disordered proteins (IDPs) comprise a variety of binding modes, from the well‐characterized folding upon binding to dynamic fuzzy complexes. To date, most studies concern the binding of an IDP to a structured protein, while the interaction between two IDPs is poorly understood. In this study, NMR, smFRET, and molecular dynamics (MD) simulation are combined to characterize the interaction between two IDPs, the C‐terminal domain (CTD) of protein 4.1G and the nuclear mitotic apparatus (NuMA) protein. It is revealed that CTD and NuMA form a fuzzy complex with remaining structural disorder. Multiple binding sites on both proteins were identified by molecular dynamics and mutagenesis studies. This study provides an atomic scenario in which two IDPs bearing multiple binding sites interact with each other in dynamic equilibrium. The combined approach employed here could be widely applicable for investigating IDPs and their dynamic interactions.</jats:p>
収録刊行物
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- Angewandte Chemie International Edition
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Angewandte Chemie International Edition 56 (26), 7515-7519, 2017-05-24
Wiley