๐ 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. 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 ร
resolution and belonged to space group P41212, with unit-cell parameters a = b = 87.2, c = 212.1 ร
. Two molecules were identified per asymmetric unit. ยฉ 2014 Cross. Mark.
author
๐ค Wang, Fenghua
๐ค Tan, Yusheng
๐ค Li, Huiyan
๐ค Chen, Xia
๐ค Wang, Jinshan
๐ค Li, Shuang
๐ค Fu, Sheng
๐ค Zhao, Qi
๐ค Chen, Cheng
๐ค Su, Dan
๐ค Yang, Haitao
year
โฐ 2014
issn
๐ 2053230X
volume
70
number
8
page
1068-1071
citedbycount
1
download
๐ [BibTeX]