7CZ4

Structure of SARS-CoV-2 macro domain in complex with ADP-ribose

7CZ4 の概要

• エントリーDOI: 10.2210/pdb7cz4/pdb
• 分子名称: Non-structural protein 3, ADENOSINE-5-DIPHOSPHORIBOSE (3 entities in total)
• 機能のキーワード: covid-19, sars-cov-2, nsp3, macro domain, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38819.69

構造登録者

Lin, M.H.,Hsu, C.H. (登録日: 2020-09-07, 公開日: 2020-11-11, 最終更新日: 2023-11-29)

主引用文献

Lin, M.H.,Chang, S.C.,Chiu, Y.C.,Jiang, B.C.,Wu, T.H.,Hsu, C.H.
Structural, Biophysical, and Biochemical Elucidation of the SARS-CoV-2 Nonstructural Protein 3 Macro Domain.
Acs Infect Dis., 6:2970-2978, 2020

PubMed Abstract: The pandemic outbreak of a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has threatened the global public health and economy since late December 2019. SARS-CoV-2 encodes the conserved macro domain within nonstructural protein 3, which may reverse cellular ADP-ribosylation and potentially cut the signal of a viral infection in the cell. Herein, we report that the SARS-CoV-2 macro domain was examined as a poly-ADP-ribose (ADPR) binding module and possessed mono-ADPR cleavage enzyme activity. After confirming the ADPR binding ability via a biophysical approach, the X-ray crystal structure of the SARS-CoV-2 macro domain was determined and structurally compared with those of other viruses. This study provides structural, biophysical, and biochemical bases to further evaluate the role of the SARS-CoV-2 macro domain in the host response via ADP-ribose binding but also as a potential target for drug design against COVID-19.

PubMed: 32946224
DOI: 10.1021/acsinfecdis.0c00441

実験手法

X-RAY DIFFRACTION (2.64 Å)