Article Information
History
- May 10, 2021.
Copyright
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
Author Information
- Juraj Ahel1,*,#,
- Adam Fletcher2,*,#,
- Daniel B. Grabarczyk1,
- Elisabeth Roitinger3,
- Luiza Deszcz1,
- Anita Lehner4,
- Satpal Virdee2,* and
- Tim Clausen1,5,*
- 1Research Institute of Molecular Pathology (IMP), Vienna BioCenter, Vienna, Austria
- 2MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom
- 3Institute of Molecular Biotechnology (IMBA), Vienna BioCenter, Vienna, Austria
- 4Vienna BioCenter Core Facilities, Vienna BioCenter, Vienna, Austria.
- 5Medical University of Vienna, Vienna, Austria
- ↵*Correspondence to: juraj.ahel{at}imp.ac.at; adam.fletcher{at}glasgow.ac.uk; s.s.virdee{at}dundee.ac.uk; tim.clausen{at}imp.ac.at
↵# These authors contributed equally to this work
Posted May 10, 2021.
E3 ubiquitin ligase RNF213 employs a non-canonical zinc finger active site and is allosterically regulated by ATP
