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The dynamics of linear polyubiquitin.
Sci. Adv. 6:eabc3786 (2020)
Polyubiquitin chains are flexible multidomain proteins, whose conformational dynamics enable them to regulate multiple biological pathways. Their dynamic is determined by the linkage between ubiquitins and by the number of ubiquitin units. Characterizing polyubiquitin behavior as a function of their length is hampered because of increasing system size and conformational variability. Here, we introduce a new approach to efficiently integrating small- angle x-ray scattering with simulations allowing us to accurately characterize the dynamics of linear di-, tri-, and tetraubiquitin in the free state as well as of diubiquitin in complex with NEMO, a central regulator in the NF-kappa B pathway. Our results show that the behavior of the diubiquitin subunits is independent of the presence of additional ubiquitin modules and that the dynamics of polyubiquitins with different lengths follow a simple model. Together with experimental data from multiple biophysical techniques, we then rationalize the 2:1 NEMO:polyubiquitin binding.
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13.116
3.374
6
14
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Nf-kappa-b; Essential Modulator Nemo; Free-energy Landscapes; Bead Form-factors; Ubiquitin Chains; Protein; Recognition; Complex; Conformations; Contributes
Language
english
Publication Year
2020
HGF-reported in Year
2020
ISSN (print) / ISBN
2375-2548
e-ISSN
2375-2548
Journal
Science Advances
Quellenangaben
Volume: 6,
Issue: 42,
Article Number: eabc3786
Publisher
American Association for the Advancement of Science (AAAS)
Publishing Place
Washington, DC [u.a.]
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-503000-001
Grants
Gauss Centre for Supercomputing e.V.
Lundbeck Foundation
DFG
European Union Seventh Framework Programme
Technische Universitat Munchen-Institute for Advanced Study - German Excellence Initiative
Lundbeck Foundation
DFG
European Union Seventh Framework Programme
Technische Universitat Munchen-Institute for Advanced Study - German Excellence Initiative
WOS ID
WOS:000579164600027
Scopus ID
85093481472
PubMed ID
33055165
Erfassungsdatum
2020-11-13