Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 616, Issue -, Pages 14-18Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2022.05.069
Keywords
ORF10; ZYG11B; Cullin-RING E3 ligase; Crystal structure
Categories
Funding
- National Natural Science Foundation of China [31900865, 32071193, 81874039]
Ask authors/readers for more resources
This study elucidates how ZYGG11B recognizes the Nterminus of ORF10, expanding the current understanding of ORF10 interaction with ZYGG11B and potentially inspiring the development of novel therapies for COVID-19.
Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARSCoV-2), has become a major threat to human health. As a unique putative protein of SARS-CoV-2, the Nterminus of ORF10 can be recognized by ZYG11B, a substrate receptor of the Cullin 2-RING E3 ubiquitin ligase (CRL2). Here we elucidated recognition mechanism of ORF10 N-terminus by ZYG11B through presenting the crystal structure of ZYG11B bound to ORF10 N-terminal peptide. Our work expands the current understanding of ORF10 interaction with ZYG11B, and may also inspire the development of novel therapies for COVID-19. (C) 2022 Elsevier Inc. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available