A new inactive conformation of SARS-CoV-2 main protease

Fornasier, E.; Macchia, M.L.; Giachin, G.; Sosic, A.; Pavan, M.; Sturlese, M.; Salata, C.; Moro, S.; Gatto, B.; Bellanda, M.; Battistutta, R.

doi:10.1107/S2059798322000948

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 8
Reshaping of the S1 and S2′ subsites. Molecular-dynamics modeling of the hypothetical interaction of new-inactive M^pro with substrates is shown. Top, putative interaction with the 11-mer pseudo-substrate peptide from PDB entry 2q6g: (a) new-inactive M^pro, (b) SARS-CoV M^pro from PDB entry 2q6g. Bottom, putative interaction with the acyl-intermediate of the M^pro C-terminal autoprocessing site: (c) new-inactive M^pro, (d) M^pro in PDB entry 7khp. As a result of the rearrangement of the oxyanion loop, a new cavity near the S2′ site, labeled `NEW', is formed.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 3| March 2022| Pages 363-378

https://doi.org/10.1107/S2059798322000948

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