Dynamically-Driven Inactivation of the Catalytic Machinery of the SARS 3C-Like Protease by the N214A...
Dynamically-Driven Inactivation of the Catalytic Machinery of the SARS 3C-Like Protease by the N214A Mutation on the Extra Domain
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United States: Public Library of Science
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English
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United States: Public Library of Science
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Contents
Despite utilizing the same chymotrypsin fold to host the catalytic machinery, coronavirus 3C-like proteases (3CLpro) noticeably differ from picornavirus 3C proteases in acquiring an extra helical domain in evolution. Previously, the extra domain was demonstrated to regulate the catalysis of the SARS-CoV 3CLpro by controlling its dimerization. Here,...
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Full title
Dynamically-Driven Inactivation of the Catalytic Machinery of the SARS 3C-Like Protease by the N214A Mutation on the Extra Domain
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TN_cdi_plos_journals_1313184907
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1313184907
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ISSN
1553-7358,1553-734X
E-ISSN
1553-7358
DOI
10.1371/journal.pcbi.1001084
