Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer

Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer

The 26S proteasome is critical for the selective degradation of proteins in eukaryotic cells. This enzyme complex is composed of approximately 70 subunits, including the structurally homologous proteins α1−α7, which combine to form heptameric rings. The correct arrangemen...

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Bibliographic Details
Main Authors: Tadashi Satoh, Maho Yagi-Utsumi, Kenta Okamoto, Eiji Kurimoto, Keiji Tanaka, Koichi Kato
Format: Article
Language:English
Published: MDPI AG 2019-05-01
Series:International Journal of Molecular Sciences
Subjects:
assembly chaperone
molecular matchmaker
molecular modeling
proteasome
X-ray crystal structure
Online Access:https://www.mdpi.com/1422-0067/20/9/2231

Internet

https://www.mdpi.com/1422-0067/20/9/2231

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