Structural insights into ORF10 recognition by ZYG11B

Biochem Biophys Res Commun. 2022 Aug 6:616:14-18. doi: 10.1016/j.bbrc.2022.05.069. Epub 2022 May 20.

Abstract

Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has become a major threat to human health. As a unique putative protein of SARS-CoV-2, the N-terminus 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.

Keywords: Crystal structure; Cullin-RING E3 ligase; ORF10; ZYG11B.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • COVID-19* / metabolism
  • COVID-19* / virology
  • Cell Cycle Proteins* / chemistry
  • Cell Cycle Proteins* / metabolism
  • Cullin Proteins
  • Humans
  • Open Reading Frames*
  • SARS-CoV-2 / chemistry
  • SARS-CoV-2 / metabolism
  • Ubiquitin-Protein Ligases* / chemistry
  • Ubiquitin-Protein Ligases* / metabolism

Substances

  • CUL2 protein, human
  • Cell Cycle Proteins
  • Cullin Proteins
  • Ubiquitin-Protein Ligases