Crystal structure of SARS-CoV 3C-like protease with baicalein

The 3C-like protease (M(pro), 3CL(pro)) plays a key role in the replication process in coronaviruses (CoVs). The M(pro) is an essential enzyme mediates CoVs replication and is a promising target for development of antiviral drugs. Until now, baicalein has been shown the specific activity for SARS-Co...

Descripción completa

Detalles Bibliográficos
Autores principales: Feng, Jingwen, Li, Dongyang, Zhang, Jin, Yin, Xiushan, Li, Jian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9027212/
https://www.ncbi.nlm.nih.gov/pubmed/35490659
http://dx.doi.org/10.1016/j.bbrc.2022.04.086
_version_ 1784691304615116800
author Feng, Jingwen
Li, Dongyang
Zhang, Jin
Yin, Xiushan
Li, Jian
author_facet Feng, Jingwen
Li, Dongyang
Zhang, Jin
Yin, Xiushan
Li, Jian
author_sort Feng, Jingwen
collection PubMed
description The 3C-like protease (M(pro), 3CL(pro)) plays a key role in the replication process in coronaviruses (CoVs). The M(pro) is an essential enzyme mediates CoVs replication and is a promising target for development of antiviral drugs. Until now, baicalein has been shown the specific activity for SARS-CoV M(pro) in vitro experiments. In this study, we resolved the SARS-CoV M(pro) with baicalein by X-ray diffraction at 2.25 Å (PDB code 7XAX), which provided a structural basis for the research and development of baicalein as an anti-CoVs drug.
format Online
Article
Text
id pubmed-9027212
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Elsevier Inc.
record_format MEDLINE/PubMed
spelling pubmed-90272122022-04-22 Crystal structure of SARS-CoV 3C-like protease with baicalein Feng, Jingwen Li, Dongyang Zhang, Jin Yin, Xiushan Li, Jian Biochem Biophys Res Commun Article The 3C-like protease (M(pro), 3CL(pro)) plays a key role in the replication process in coronaviruses (CoVs). The M(pro) is an essential enzyme mediates CoVs replication and is a promising target for development of antiviral drugs. Until now, baicalein has been shown the specific activity for SARS-CoV M(pro) in vitro experiments. In this study, we resolved the SARS-CoV M(pro) with baicalein by X-ray diffraction at 2.25 Å (PDB code 7XAX), which provided a structural basis for the research and development of baicalein as an anti-CoVs drug. Elsevier Inc. 2022-06-30 2022-04-22 /pmc/articles/PMC9027212/ /pubmed/35490659 http://dx.doi.org/10.1016/j.bbrc.2022.04.086 Text en © 2022 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Feng, Jingwen
Li, Dongyang
Zhang, Jin
Yin, Xiushan
Li, Jian
Crystal structure of SARS-CoV 3C-like protease with baicalein
title Crystal structure of SARS-CoV 3C-like protease with baicalein
title_full Crystal structure of SARS-CoV 3C-like protease with baicalein
title_fullStr Crystal structure of SARS-CoV 3C-like protease with baicalein
title_full_unstemmed Crystal structure of SARS-CoV 3C-like protease with baicalein
title_short Crystal structure of SARS-CoV 3C-like protease with baicalein
title_sort crystal structure of sars-cov 3c-like protease with baicalein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9027212/
https://www.ncbi.nlm.nih.gov/pubmed/35490659
http://dx.doi.org/10.1016/j.bbrc.2022.04.086
work_keys_str_mv AT fengjingwen crystalstructureofsarscov3clikeproteasewithbaicalein
AT lidongyang crystalstructureofsarscov3clikeproteasewithbaicalein
AT zhangjin crystalstructureofsarscov3clikeproteasewithbaicalein
AT yinxiushan crystalstructureofsarscov3clikeproteasewithbaicalein
AT lijian crystalstructureofsarscov3clikeproteasewithbaicalein

Ejemplares similares