The dynamic multisite interactions between two intrinsically disordered proteins

Handle URI:
http://hdl.handle.net/10754/623649
Title:
The dynamic multisite interactions between two intrinsically disordered proteins
Authors:
Wu, Shaowen; Wang, Dongdong; Liu, Jin; Feng, Yitao; Weng, Jingwei; Li, Yu; Gao, Xin ( 0000-0002-7108-3574 ) ; Liu, Jianwei; Wang, Wenning
Abstract:
Protein 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.
KAUST Department:
King Abdullah University of Science and Technology; SAUDI ARABIA
Citation:
Wu 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.
Publisher:
Wiley-Blackwell
Journal:
Angewandte Chemie International Edition
Issue Date:
11-May-2017
DOI:
10.1002/anie.201701883; 10.1002/ange.201701883
Type:
Article
ISSN:
1433-7851
Sponsors:
This 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.
Additional Links:
http://onlinelibrary.wiley.com/doi/10.1002/anie.201701883/abstract
Appears in Collections:
Articles

Full metadata record

DC FieldValue Language
dc.contributor.authorWu, Shaowenen
dc.contributor.authorWang, Dongdongen
dc.contributor.authorLiu, Jinen
dc.contributor.authorFeng, Yitaoen
dc.contributor.authorWeng, Jingweien
dc.contributor.authorLi, Yuen
dc.contributor.authorGao, Xinen
dc.contributor.authorLiu, Jianweien
dc.contributor.authorWang, Wenningen
dc.date.accessioned2017-05-17T07:41:40Z-
dc.date.available2017-05-17T07:41:40Z-
dc.date.issued2017-05-11en
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.en
dc.identifier.issn1433-7851en
dc.identifier.doi10.1002/anie.201701883en
dc.identifier.doi10.1002/ange.201701883en
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.en
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.en
dc.publisherWiley-Blackwellen
dc.relation.urlhttp://onlinelibrary.wiley.com/doi/10.1002/anie.201701883/abstracten
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.en
dc.subjectNMRen
dc.subjectMD simulationen
dc.subjectIntrinsically Disordered Proteinen
dc.subjectCtd Of Protein 4.1en
dc.subjectSmfreten
dc.titleThe dynamic multisite interactions between two intrinsically disordered proteinsen
dc.typeArticleen
dc.contributor.departmentKing Abdullah University of Science and Technology; SAUDI ARABIAen
dc.identifier.journalAngewandte Chemie International Editionen
dc.eprint.versionPost-printen
dc.contributor.institutionFudan University; Chemistry; CHINAen
dc.contributor.institutionCHINAen
dc.contributor.institutionFudan University; Chemistry; Shanghai CHINAen
dc.contributor.institutionFudan University; Department of Chemistry; 220 Handan Road 200433 Shanghai CHINAen
kaust.authorLi, Yuen
kaust.authorGao, Xinen
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