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dc.contributor.authorWu, Shaowen
dc.contributor.authorWang, Dongdong
dc.contributor.authorLiu, Jin
dc.contributor.authorFeng, Yitao
dc.contributor.authorWeng, Jingwei
dc.contributor.authorLi, Yu
dc.contributor.authorGao, Xin
dc.contributor.authorLiu, Jianwei
dc.contributor.authorWang, Wenning
dc.date.accessioned2017-05-17T07:41:40Z
dc.date.available2017-05-17T07:41:40Z
dc.date.issued2017-05-24
dc.identifier.citationWu S, Wang D, Liu J, Feng Y, Weng J, et al. (2017) The dynamic multisite interactions between two intrinsically disordered proteins. Angewandte Chemie International Edition. Available: http://dx.doi.org/10.1002/anie.201701883.
dc.identifier.issn1433-7851
dc.identifier.doi10.1002/anie.201701883
dc.identifier.doi10.1002/ange.201701883
dc.identifier.urihttp://hdl.handle.net/10754/623649
dc.description.abstractProtein interactions involving intrinsically disordered proteins (IDPs) comprise a variety of binding modes, from the well characterized folding upon binding to dynamic fuzzy complex. 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, we combined NMR, smFRET, and molecular dynamics (MD) simulation 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 MD and mutagenesis studies. Our 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.
dc.description.sponsorshipThis work was supported by National Major Basic Research Program of China (2016YFA0501702), National Science Foundation of China (21473034, 21375028, 21273188), Specialized Research Fund for the Doctoral Program of Higher Education (20130071140004). X. G. and Y. L. thanks the support by funding from King Abdullah University of Science and Technology (KAUST). This research made use of the resources of the computer clusters at KAUST and the computer center at Fudan University.
dc.publisherWiley
dc.relation.urlhttp://onlinelibrary.wiley.com/doi/10.1002/anie.201701883/abstract
dc.rightsThis is the peer reviewed version of the following article: The dynamic multisite interactions between two intrinsically disordered proteins, which has been published in final form at http://doi.org/10.1002/anie.201701883. This article may be used for non-commercial purposes in accordance With Wiley Terms and Conditions for self-archiving.
dc.subjectNMR
dc.subjectMD simulation
dc.subjectIntrinsically Disordered Protein
dc.subjectCtd Of Protein 4.1
dc.subjectSmfret
dc.titleThe dynamic multisite interactions between two intrinsically disordered proteins
dc.typeArticle
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
dc.contributor.departmentComputer Science Program
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.identifier.journalAngewandte Chemie International Edition
dc.eprint.versionPost-print
dc.contributor.institutionFudan University; Chemistry; CHINA
dc.contributor.institutionCHINA
dc.contributor.institutionFudan University; Chemistry; Shanghai CHINA
dc.contributor.institutionFudan University; Department of Chemistry; 220 Handan Road 200433 Shanghai CHINA
kaust.personLi, Yu
kaust.personGao, Xin
refterms.dateFOA2018-05-11T00:00:00Z
kaust.acknowledged.supportUnitcomputer clusters at KAUST
dc.date.published-online2017-05-24
dc.date.published-print2017-06-19


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