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Structural view of the 2A protease from human rhinovirus C15
Author(s) -
Ling Hui,
Yang Pan,
Hou Hai,
Sun Yao
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18003382
Subject(s) - rhinovirus , protease , affinity chromatography , binding site , chemistry , coxsackievirus , size exclusion chromatography , biology , stereochemistry , virology , enzyme , virus , biochemistry , enterovirus
The majority of outbreaks of the common cold are caused by rhinoviruses. The 2A protease (2A pro ) of human rhinoviruses (HRVs) is known to play important roles in the propagation of the virus and the modulation of host signal pathways to facilitate viral replication. The 2A pro from human rhinovirus C15 (HRV‐C15) has been expressed in Escherichia coli and purified by affinity chromatography, ion‐exchange chromatography and gel‐filtration chromatography. The crystals diffracted to 2.6 Å resolution. The structure was solved by molecular replacement using the structure of 2A pro from coxsackievirus A16 (CVA16) as the search model. The structure contains a conserved His–Asp–Cys catalytic triad and a Zn 2+ ‐binding site. Comparison with other 2A pro structures from enteroviruses reveals that the substrate‐binding cleft of 2A pro from HRV‐C15 exhibits a more open conformation, which presumably favours substrate binding.