ArticleActa crystallographica. Section F, Structural biology communications2014
1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Chaperones shape the conformational landscape of 26S-proteasome-base assembly for allosteric ATPase motor activation.bioRxiv : the preprint server for biology · 2026Article
- Proteasome subunit PSMC3 variants cause neurosensory syndrome combining deafness and cataract due to proteotoxic stress.EMBO molecular medicine · 2020Article
- Cooperativity in Proteasome Core Particle Maturation.iScience · 2020Article
- Ubiquitin-dependent switch during assembly of the proteasomal ATPases mediated by Not4 ubiquitin ligase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.
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