Mechanism of the Rpn13-induced activation of Uch37

@inproceedings{Jiao2014MechanismOT,
  title={Mechanism of the Rpn13-induced activation of Uch37},
  author={Lianying Jiao and Songying Ouyang and Neil A. Shaw and Gaojie Song and Yingang Feng and Fengfeng Niu and Weicheng Qiu and Hongtao Zhu and Li-wei Hung and Xiaobing Zuo and V. Eleonora Shtykova and Ping Zhu and Yuhui Dong and Ruxiang Xu and Zhi-Jie Liu},
  booktitle={Protein & Cell},
  year={2014}
}
Uch37 is a de-ubiquitinating enzyme that is activated by Rpn13 and involved in the proteasomal degradation of proteins. The full-length Uch37 was shown to exhibit low iso-peptidase activity and is thought to be auto-inhibited. Structural comparisons revealed that within a homo-dimer of Uch37, each of the catalytic domains was blocking the other’s ubiquitin (Ub)-binding site. This blockage likely prevented Ub from entering the active site of Uch37 and might form the basis of auto-inhibition. To… CONTINUE READING