The Human Otubain2-Ubiquitin Structure Provides Insights into the Cleavage Specificity of Poly-Ubiquitin-Linkages

@inproceedings{Altun2015TheHO,
  title={The Human Otubain2-Ubiquitin Structure Provides Insights into the Cleavage Specificity of Poly-Ubiquitin-Linkages},
  author={Mikael Altun and Thomas S Walter and Holger B. Kramer and Patrick Herr and Alexander Iphoefer and Johan Bostr{\"o}m and Yael David and Alia Komsany and Nicola Ternette and Ami Navon and David I Stuart and Jingshan Ren and Benedikt M. Kessler},
  booktitle={PloS one},
  year={2015}
}
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 otubains (vOTUs) bind ubiquitin/ISG15, and more similar to yeast and mammalian OTUs. In contrast to OTUB1 which has exclusive specificity towards Lys48 poly-ubiquitin chains, OTUB2 cleaves different… CONTINUE READING