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Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor

Human coronavirus NL63 mainly infects younger children and causes cough, fever, rhinorrhoea, bronchiolitis and croup. It encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits...

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Autores principales: Wang, Fenghua, Tan, Yusheng, Li, Huiyan, Chen, Xia, Wang, Jinshan, Li, Shuang, Fu, Sheng, Zhao, Qi, Chen, Cheng, Su, Dan, Yang, Haitao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4118806/
https://www.ncbi.nlm.nih.gov/pubmed/25084384
http://dx.doi.org/10.1107/S2053230X14012953
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author Wang, Fenghua
Tan, Yusheng
Li, Huiyan
Chen, Xia
Wang, Jinshan
Li, Shuang
Fu, Sheng
Zhao, Qi
Chen, Cheng
Su, Dan
Yang, Haitao
author_facet Wang, Fenghua
Tan, Yusheng
Li, Huiyan
Chen, Xia
Wang, Jinshan
Li, Shuang
Fu, Sheng
Zhao, Qi
Chen, Cheng
Su, Dan
Yang, Haitao
author_sort Wang, Fenghua
collection PubMed
description Human coronavirus NL63 mainly infects younger children and causes cough, fever, rhinorrhoea, bronchiolitis and croup. It encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of human coronavirus NL63 was crystallized in complex with a Michael acceptor. The complex crystals diffracted to 2.85 Å resolution and belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 87.2, c = 212.1 Å. Two molecules were identified per asymmetric unit.
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spelling pubmed-41188062016-08-01 Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor Wang, Fenghua Tan, Yusheng Li, Huiyan Chen, Xia Wang, Jinshan Li, Shuang Fu, Sheng Zhao, Qi Chen, Cheng Su, Dan Yang, Haitao Acta Crystallogr F Struct Biol Commun Crystallization Communications Human coronavirus NL63 mainly infects younger children and causes cough, fever, rhinorrhoea, bronchiolitis and croup. It encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of human coronavirus NL63 was crystallized in complex with a Michael acceptor. The complex crystals diffracted to 2.85 Å resolution and belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 87.2, c = 212.1 Å. Two molecules were identified per asymmetric unit. International Union of Crystallography 2014-07-23 /pmc/articles/PMC4118806/ /pubmed/25084384 http://dx.doi.org/10.1107/S2053230X14012953 Text en © International Union of Crystallography 2014
spellingShingle Crystallization Communications
Wang, Fenghua
Tan, Yusheng
Li, Huiyan
Chen, Xia
Wang, Jinshan
Li, Shuang
Fu, Sheng
Zhao, Qi
Chen, Cheng
Su, Dan
Yang, Haitao
Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor
title Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor
title_full Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor
title_fullStr Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor
title_full_unstemmed Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor
title_short Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor
title_sort crystallization and preliminary crystallographic study of human coronavirus nl63 main protease in complex with an inhibitor
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4118806/
https://www.ncbi.nlm.nih.gov/pubmed/25084384
http://dx.doi.org/10.1107/S2053230X14012953
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