Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs

David Haselbach; Jil Schrader; Felix Lambrecht; Fabian Henneberg; Ashwin Chari; Holger Stark

doi:10.1038/ncomms15578

Nature Communications (May 2017)

Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs

David Haselbach,
Jil Schrader,
Felix Lambrecht,
Fabian Henneberg,
Ashwin Chari,
Holger Stark

Affiliations

David Haselbach: Department for Structural Dynamics, Max-Planck Institute for Biophysical Chemistry
Jil Schrader: Department for Structural Dynamics, Max-Planck Institute for Biophysical Chemistry
Felix Lambrecht: Department for Structural Dynamics, Max-Planck Institute for Biophysical Chemistry
Fabian Henneberg: Department for Structural Dynamics, Max-Planck Institute for Biophysical Chemistry
Ashwin Chari: Department for Structural Dynamics, Max-Planck Institute for Biophysical Chemistry
Holger Stark: Department for Structural Dynamics, Max-Planck Institute for Biophysical Chemistry

DOI: https://doi.org/10.1038/ncomms15578
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 8

Abstract

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The proteasome regulates several important cellular processes and has been identified as a target for therapeutic interventions. Here the authors map the conformational and energy landscape of the 26S proteasome upon Oprozomib binding and uncover long-range allosteric effects that control the dynamic behaviour of the proteasome.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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