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Alternative modes of client binding enable functional plasticity of Hsp70

Author

Listed:
  • Alireza Mashaghi

    (FOM institute AMOLF)

  • Sergey Bezrukavnikov

    (FOM institute AMOLF)

  • David P. Minde

    (FOM institute AMOLF)

  • Anne S. Wentink

    (Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

  • Roman Kityk

    (Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance)

  • Beate Zachmann-Brand

    (Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

  • Matthias P. Mayer

    (Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance)

  • Günter Kramer

    (Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

  • Bernd Bukau

    (Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

  • Sander J. Tans

    (FOM institute AMOLF)

Abstract

Hsp70 binds unfolded protein segments in its groove, but can also bind and stabilize folded protein structures, owing to its moveable lid, with ATP hydrolysis and co-chaperones allowing control of these contrasting effects.

Suggested Citation

  • Alireza Mashaghi & Sergey Bezrukavnikov & David P. Minde & Anne S. Wentink & Roman Kityk & Beate Zachmann-Brand & Matthias P. Mayer & Günter Kramer & Bernd Bukau & Sander J. Tans, 2016. "Alternative modes of client binding enable functional plasticity of Hsp70," Nature, Nature, vol. 539(7629), pages 448-451, November.
    • Handle: RePEc:nat:nature:v:539:y:2016:i:7629:d:10.1038_nature20137
    DOI: 10.1038/nature20137
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    Cited by:

    1. Dezerae Cox & Ching-Seng Ang & Nadinath B. Nillegoda & Gavin E. Reid & Danny M. Hatters, 2022. "Hidden information on protein function in censuses of proteome foldedness," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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