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Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2

Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_6a9a3ed39ff54d0fae4c92979ac96f5c

Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2

About this item

Full title

Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2018-09, Vol.9 (1), p.3669-14, Article 3669

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Disordered extensions at the termini and short internal insertions distinguish eukaryotic ribosomal proteins (r-proteins) from their anucleated archaeal counterparts. Here, we report an NMR structure of such a eukaryotic-specific segment (ESS) in the r-protein eS26 in complex with the escortin Tsr2. The structure reveals how ESS attracts Tsr2 speci...

Alternative Titles

Full title

Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_6a9a3ed39ff54d0fae4c92979ac96f5c

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_6a9a3ed39ff54d0fae4c92979ac96f5c

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-018-06160-x

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