Log in to save to my catalogue

Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_665259f0303c4a7a8d8b890e1f4e21c3

Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

About this item

Full title

Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2018-10, Vol.9 (1), p.4441-12, Article 4441

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Deregulation of the ubiquitin ligase E6AP is causally linked to the development of human disease, including cervical cancer. In complex with the E6 oncoprotein of human papillomaviruses, E6AP targets the tumor suppressor p53 for degradation, thereby contributing to carcinogenesis. Moreover, E6 acts as a potent activator of E6AP by a yet unknown mec...

Alternative Titles

Full title

Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_665259f0303c4a7a8d8b890e1f4e21c3

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_665259f0303c4a7a8d8b890e1f4e21c3

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-018-06953-0

How to access this item