7E6R

Crystal structure of HCoV-NL63 3C-like protease,pH5.6

7E6R の概要

• エントリーDOI: 10.2210/pdb7e6r/pdb
• 分子名称: 3C-like proteinase (2 entities in total)
• 機能のキーワード: hcov-nl63 3c-like protease, viral protein
• 由来する生物種: Human coronavirus NL63 (HCoV-NL63)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65526.26

構造登録者

Gao, H.X.,Zhang, Y.T.,Zhong, F.L.,Zhou, X.L.,Li, J.,Zhang, J. (登録日: 2021-02-23, 公開日: 2021-10-06, 最終更新日: 2023-11-29)

主引用文献

Gao, H.,Zhang, Y.,Jiang, H.,Hu, X.,Zhang, Y.,Zhou, X.,Zhong, F.,Lin, C.,Li, J.,Luo, J.,Zhang, J.
Crystal structures of human coronavirus NL63 main protease at different pH values
Acta Crystallogr.,Sect.F, 77:348-355, 2021

PubMed Abstract: Human coronavirus NL63 (HCoV-NL63), which belongs to the genus Alphacoronavirus, mainly infects children and the immunocompromized and is responsible for a series of clinical manifestations, including cough, fever, rhinorrhoea, bronchiolitis and croup. HCoV-NL63, which was first isolated from a seven-month-old child in 2004, has led to infections worldwide and accounts for 10% of all respiratory illnesses caused by etiological agents. However, effective antivirals against HCoV-NL63 infection are currently unavailable. The HCoV-NL63 main protease (M), also called 3C-like protease (3CL), plays a vital role in mediating viral replication and transcription by catalyzing the cleavage of replicase polyproteins (pp1a and pp1ab) into functional subunits. Moreover, M is highly conserved among all coronaviruses, thus making it a prominent drug target for antiviral therapy. Here, four crystal structures of HCoV-NL63 M in the apo form at different pH values are reported at resolutions of up to 1.78 Å. Comparison with M from other human betacoronaviruses such as SARS-CoV-2 and SARS-CoV reveals common and distinct structural features in different genera and extends knowledge of the diversity, function and evolution of coronaviruses.

PubMed: 34605439
DOI: 10.1107/S2053230X21009523

実験手法

X-RAY DIFFRACTION (1.9 Å)