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RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_817fe8022b364f6ab87e9c148af5e6d8

RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

About this item

Full title

RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2018-04, Vol.9 (1), p.1501-13, Article 1501

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

Subjects

Subjects and topics

More information

Scope and Contents

Contents

The R2TP/Prefoldin-like co-chaperone, in concert with HSP90, facilitates assembly and cellular stability of RNA polymerase II, and complexes of PI3-kinase-like kinases such as mTOR. However, the mechanism by which this occurs is poorly understood. Here we use cryo-EM and biochemical studies on the human R2TP core (RUVBL1–RUVBL2–RPAP3–PIH1D1) which...

Alternative Titles

Full title

RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_817fe8022b364f6ab87e9c148af5e6d8

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_817fe8022b364f6ab87e9c148af5e6d8

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-018-03942-1

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