The human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages.

The human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages.

Ovarian tumor domain containing proteases cleave ubiquitin (Ub) and ubiquitin-like polypeptides from proteins. Here we report the crystal structure of human otubain 2 (OTUB2) in complex with a ubiquitin-based covalent inhibitor, Ub-Br2. The ubiquitin binding mode is oriented differently to how viral...

Full description

Saved in:
Bibliographic Details
Main Authors: Mikael Altun, Thomas S Walter, Holger B Kramer, Patrick Herr, Alexander Iphöfer, Johan Boström, Yael David, Alia Komsany, Nicola Ternette, Ami Navon, David I Stuart, Jingshan Ren, Benedikt M Kessler
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0115344
Tags: Add Tag
No Tags, Be the first to tag this record!

Internet

https://doi.org/10.1371/journal.pone.0115344

Similar Items