The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1

TRAF6 is a RING E3 ligase that builds Lys63-linked ubiquitin chains. Here, the authors present the crystal structure of TRAF6 bound to the Ubc13~Ub conjugate, which, together with biochemical assays, reveals the role of the zinc finger domains and why RING dimerisation is required for TRAF6 activity...

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Main Authors: Adam J. Middleton, Rhesa Budhidarmo, Anubrita Das, Jingyi Zhu, Martina Foglizzo, Peter D. Mace, Catherine L. Day
Format: Article
Language:English
Published: Nature Publishing Group 2017-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-01665-3
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spelling doaj-ddb61465d25e4a88871e1ae208a5f36f2021-05-11T07:39:56ZengNature Publishing GroupNature Communications2041-17232017-11-018111010.1038/s41467-017-01665-3The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1Adam J. Middleton0Rhesa Budhidarmo1Anubrita Das2Jingyi Zhu3Martina Foglizzo4Peter D. Mace5Catherine L. Day6Department of Biochemistry, School of Biomedical Sciences, University of OtagoDepartment of Biochemistry, School of Biomedical Sciences, University of OtagoDepartment of Biochemistry, School of Biomedical Sciences, University of OtagoDepartment of Biochemistry, School of Biomedical Sciences, University of OtagoDepartment of Biochemistry, School of Biomedical Sciences, University of OtagoDepartment of Biochemistry, School of Biomedical Sciences, University of OtagoDepartment of Biochemistry, School of Biomedical Sciences, University of OtagoTRAF6 is a RING E3 ligase that builds Lys63-linked ubiquitin chains. Here, the authors present the crystal structure of TRAF6 bound to the Ubc13~Ub conjugate, which, together with biochemical assays, reveals the role of the zinc finger domains and why RING dimerisation is required for TRAF6 activity.https://doi.org/10.1038/s41467-017-01665-3
collection DOAJ
language English
format Article
sources DOAJ
author Adam J. Middleton
Rhesa Budhidarmo
Anubrita Das
Jingyi Zhu
Martina Foglizzo
Peter D. Mace
Catherine L. Day
spellingShingle Adam J. Middleton
Rhesa Budhidarmo
Anubrita Das
Jingyi Zhu
Martina Foglizzo
Peter D. Mace
Catherine L. Day
The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1
Nature Communications
author_facet Adam J. Middleton
Rhesa Budhidarmo
Anubrita Das
Jingyi Zhu
Martina Foglizzo
Peter D. Mace
Catherine L. Day
author_sort Adam J. Middleton
title The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1
title_short The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1
title_full The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1
title_fullStr The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1
title_full_unstemmed The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1
title_sort activity of traf ring homo- and heterodimers is regulated by zinc finger 1
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-11-01
description TRAF6 is a RING E3 ligase that builds Lys63-linked ubiquitin chains. Here, the authors present the crystal structure of TRAF6 bound to the Ubc13~Ub conjugate, which, together with biochemical assays, reveals the role of the zinc finger domains and why RING dimerisation is required for TRAF6 activity.
url https://doi.org/10.1038/s41467-017-01665-3
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