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Ubiquitin chain conformation regulates recognition and activity of interacting proteins

Author

Listed:
  • Yu Ye

    (MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK)

  • Georg Blaser

    (University of Cambridge, Cambridge CB2 1EW, UK)

  • Mathew H. Horrocks

    (University of Cambridge, Cambridge CB2 1EW, UK)

  • Maria J. Ruedas-Rama

    (Faculty of Pharmacy, University of Granada, Campus Cartuja, 18071 Granada, Spain)

  • Shehu Ibrahim

    (University of Cambridge, Cambridge CB2 1EW, UK)

  • Alexander A. Zhukov

    (University of Cambridge, Cambridge CB2 1EW, UK)

  • Angel Orte

    (Faculty of Pharmacy, University of Granada, Campus Cartuja, 18071 Granada, Spain)

  • David Klenerman

    (University of Cambridge, Cambridge CB2 1EW, UK)

  • Sophie E. Jackson

    (University of Cambridge, Cambridge CB2 1EW, UK)

  • David Komander

    (MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK)

Abstract

Single-molecule FRET assays used to probe the conformational dynamics of ubiquitin chains reveal that conformational selection is an important mechanism of ubiquitin chain recognition.

Suggested Citation

  • Yu Ye & Georg Blaser & Mathew H. Horrocks & Maria J. Ruedas-Rama & Shehu Ibrahim & Alexander A. Zhukov & Angel Orte & David Klenerman & Sophie E. Jackson & David Komander, 2012. "Ubiquitin chain conformation regulates recognition and activity of interacting proteins," Nature, Nature, vol. 492(7428), pages 266-270, December.
    • Handle: RePEc:nat:nature:v:492:y:2012:i:7428:d:10.1038_nature11722
    DOI: 10.1038/nature11722
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