Human 26S proteasome bound to the chemotherapeutic Oprozomib
Ontology highlight
ABSTRACT:
SUBMITTER: David Haselbach
PROVIDER: EMPIAR-10166 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs.
Haselbach David D Schrader Jil J Lambrecht Felix F Henneberg Fabian F Chari Ashwin A Stark Holger H
Nature communications 20170525
The proteasome holoenzyme is the major non-lysosomal protease; its proteolytic activity is essential for cellular homeostasis. Thus, it is an attractive target for the development of chemotherapeutics. While the structural basis of core particle (CP) inhibitors is largely understood, their structural impact on the proteasome holoenzyme remains entirely elusive. Here, we determined the structure of the 26S proteasome with and without the inhibitor Oprozomib. Drug binding modifies the energy lands ...[more]
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