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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2014
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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. |
format | Online Article Text |
id | pubmed-4118806 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
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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