4.6 Article

Structural insights into ORF10 recognition by ZYG11B

Journal

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2022.05.069

Keywords

ORF10; ZYG11B; Cullin-RING E3 ligase; Crystal structure

Funding

  1. National Natural Science Foundation of China [31900865, 32071193, 81874039]

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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.

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