Allosteric coupling between α-rings of the 20S proteasome
The 26S proteasome is a protein degradation machine composed of a 20S core particle (CP) flanked at one or both ends by a 19S ATPase regulatory particle (RP). Here the authors reconstitute asymmetric archaeal proteasomes and reveal allosteric coupling between the conformations of gates in the α-ring...
Main Authors: | Zanlin Yu, Yadong Yu, Feng Wang, Alexander G. Myasnikov, Philip Coffino, Yifan Cheng |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2020-09-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-18415-7 |
Similar Items
-
Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs
by: David Haselbach, et al.
Published: (2017-05-01) -
Structural Fluctuations of the Human Proteasome α7 Homo-Tetradecamer Double Ring Imply the Proteasomal α-Ring Assembly Mechanism
by: Chihong Song, et al.
Published: (2021-04-01) -
Ubiquitin Proteasome System in Stress and Disease
by: Dmitry Karpov, et al.
Published: (2012-01-01) -
Interplay between Structure and Charge as a Key to Allosteric Modulation of Human 20S Proteasome by the Basic Fragment of HIV-1 Tat Protein.
by: Przemysław Karpowicz, et al.
Published: (2015-01-01) -
Study on the molecular mechanism of the interaction between 20S proteasome and proteasome activating nucleotidase
by: Chia-Pei Chen, et al.
Published: (2008)