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Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4

Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_4244723ac5d244baa41f569db4a6c956

Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4

About this item

Full title

Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2019-12, Vol.10 (1), p.5708-13, Article 5708

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Npl4 is likely to be the most upstream factor recognizing Lys48-linked polyubiquitylated substrates in the proteasomal degradation pathway in yeast. Along with Ufd1, Npl4 forms a heterodimer (UN), and functions as a cofactor for the Cdc48 ATPase. Here, we report the crystal structures of yeast Npl4 in complex with Lys48-linked diubiquitin and with...

Alternative Titles

Full title

Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_4244723ac5d244baa41f569db4a6c956

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_4244723ac5d244baa41f569db4a6c956

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-019-13697-y

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