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  Allosteric switch regulates protein–protein binding through collective motion.

Smith, C. A., Ban, D., Pratihar, S., Giller, K., Paulat, M., Becker, S., et al. (2016). Allosteric switch regulates protein–protein binding through collective motion. Proceedings of the National Academy of Sciences of the United States of America, 113(12), 3269-3274. doi:10.1073/pnas.1519609113.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-226C-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-1FF6-2
Genre: Journal Article

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 Creators:
Smith, C. A.1, Author              
Ban, D.2, Author              
Pratihar, S.2, Author              
Giller, K.2, Author              
Paulat, M.2, Author              
Becker, S.2, Author              
Griesinger, C.2, Author              
Lee, D.2, Author              
de Groot, B. L.1, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              
2Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: Allostery; Protein dynamics; Concerted motion; Relaxation dispersion; Nuclear magnetic resonance
 Abstract: Many biological processes depend on allosteric communication between different parts of a protein, but the role of internal protein motion in propagating signals through the structure remains largely unknown. Through an experimental and computational analysis of the ground state dynamics in ubiquitin, we identify a collective global motion that is specifically linked to a conformational switch distant from the binding interface. This allosteric coupling is also present in crystal structures and is found to facilitate multispecificity, particularly binding to the ubiquitin-specific protease (USP) family of deubiquitinases. The collective motion that enables this allosteric communication does not affect binding through localized changes but, instead, depends on expansion and contraction of the entire protein domain. The characterization of these collective motions represents a promising avenue for finding and manipulating allosteric networks.

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Language(s): eng - English
 Dates: 2016-03-22
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1519609113
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 113 (12) Sequence Number: - Start / End Page: 3269 - 3274 Identifier: -