liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Solution NMR structure of the TRIM21 B-box2 and identification of residues involved in its interaction with the RING domain
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering. MRC, England.
University of Toronto, Canada; University of Toronto, Canada.
Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics. Linköping University, Faculty of Science & Engineering.
Show others and affiliations
2017 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 12, no 7, article id e0181551Article in journal (Refereed) Published
Abstract [en]

Tripartite motif-containing (TRIM) proteins are defined by the sequential arrangement of RING, B-box and coiled-coil domains (RBCC), where the B-box domain is a unique feature of the TRIM protein family. TRIM21 is an E3 ubiquitin-protein ligase implicated in innate immune signaling by acting as an autoantigen and by modifying interferon regulatory factors. Here we report the three-dimensional solution structure of the TRIM21 B-box2 domain by nuclear magnetic resonance (NMR) spectroscopy. The structure of the B-box2 domain, comprising TRIM21 residues 86-130, consists of a short alpha-helical segment with an N-terminal short beta-strand and two anti-parallel beta-strands jointly found the core, and adopts a RING-like fold. This beta beta alpha beta core largely defines the overall fold of the TRIM21 B-box2 and the coordination of one Zn2+ ion stabilizes the tertiary structure of the protein. Using NMR titration experiments, we have identified an exposed interaction surface, a novel interaction patch where the B-box2 is likely to bind the N-terminal RING domain. Our structure together with comparisons with other TRIM B-box domains jointly reveal how its different surfaces are employed for various modular interactions, and provides extended understanding of how this domain relates to flanking domains in TRIM proteins.

Place, publisher, year, edition, pages
PUBLIC LIBRARY SCIENCE , 2017. Vol. 12, no 7, article id e0181551
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:liu:diva-139915DOI: 10.1371/journal.pone.0181551ISI: 000406579300020PubMedID: 28753623OAI: oai:DiVA.org:liu-139915DiVA, id: diva2:1135448
Note

Funding Agencies|Swedish Science Council; Swedish Cancer Foundation; Swedish Foundation for International Cooperation in Research and Higher Education

Available from: 2017-08-23 Created: 2017-08-23 Last updated: 2017-11-29

Open Access in DiVA

fulltext(11138 kB)27 downloads
File information
File name FULLTEXT01.pdfFile size 11138 kBChecksum SHA-512
c69a849ae55bfb43571b9f2a218c75e56f6ef5d07c7b4ba7e09d0ee73e3085f09df8cd0f22eafd2034ded278138684add5ae9a7cc523b6b923a9bc3b9f1b472b
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Wallenhammar, AmélieAnandapadmanaban, MadhanagopalMirabello, ClaudioLundström, PatrikWallner, BjörnSunnerhagen, Maria
By organisation
ChemistryFaculty of Science & EngineeringBioinformatics
In the same journal
PLoS ONE
Structural Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 27 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 116 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf