Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP

Benjamin Stieglitz, Rohini R. Rana, Marios G. Koliopoulos, Aylin C. Morris-Davies, Veronique Schaeffer, Evangelos Christodoulou, Steven Howell, Nicholas R. Brown, Ivan Dikic and Katrin Rittinger ()
Additional contact information
Benjamin Stieglitz: MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK
Rohini R. Rana: MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK
Marios G. Koliopoulos: MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK
Aylin C. Morris-Davies: MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK
Veronique Schaeffer: Institute of Biochemistry II, Goethe University, School of Medicine, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany
Evangelos Christodoulou: MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK
Steven Howell: MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK
Nicholas R. Brown: MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK
Ivan Dikic: Institute of Biochemistry II, Goethe University, School of Medicine, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany
Katrin Rittinger: MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK

Nature, 2013, vol. 503, issue 7476, 422-426

Abstract: The crystal structure of a complex between the catalytic core of the HOIP subunit of the E3 ligase LUBAC and ubiquitin is reported, yielding insight into the ubiquitin transfer reaction and explaining how HOIP is capable of synthesizing linear ubiquitin chains with high specificity.

Date: 2013
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/nature12638 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:503:y:2013:i:7476:d:10.1038_nature12638

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature12638

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().