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Article

New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 Å resolution.

Acta crystallographica. Section F, Structural biology and crystallization communications - 1 May 2012

Kim Sangwoo, Nishide Akira, Saeki Yasushi, Takagi Kenji, Tanaka Keiji, Kato Koichi, Mizushima Tsunehiro

Abstract excerpt

The 26S proteasome is an ATP-dependent protease responsible for selective degradation of polyubiquitylated proteins. Recent studies have suggested that proteasome assembly is a highly ordered multi-step process assisted by specific chaperones. Rpn14, an assembly chaperone for ATPase-ring formation, specifically recognizes the ATPase subunit Rpt6. The structure of Rpn14 at 2.0 Å resolution in space group P6(4) has...

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Identifiers

PMID: 22691779
DOI: 10.1107/S1744309112011359
PMCID: PMC3374504

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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