Allosteric switch regulates protein–protein binding through collective motion.

Smith, C. A.; Ban, D.; Pratihar, S.; Giller, K.; Paulat, M.; Becker, S.; Griesinger, C.; Lee, D.; de Groot, B. L.

doi:10.1073/pnas.1519609113

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学術論文

Allosteric switch regulates protein–protein binding through collective motion.

MPS-Authors

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Smith, C. A.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Ban, D.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons135836

Pratihar, S.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Giller, K.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons142048

Paulat, M.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14824

Becker, S.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15147

Griesinger, C.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15424

Lee, D.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14970

de Groot, B. L.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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http://www.pnas.org/content/113/12/3269.full.pdf
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2262648_Suppl.pdf
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引用

Smith, C. A., Ban, D., Pratihar, S., Giller, K., Paulat, M., Becker, S., Griesinger, C., Lee, D., & de Groot, B. L. (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.

引用: https://hdl.handle.net/11858/00-001M-0000-002A-226C-0

要旨

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.