Literature summary for 3.4.22.B80 extracted from

Pitsillou, E.; Liang, J.; Hung, A.; Karagiannis, T.C.
Inhibition of interferon-stimulated gene 15 and lysine 48-linked ubiquitin binding to the SARS-CoV-2 papain-like protease by small molecules In silico studies (2021), Chem. Phys. Lett., 771, 138468 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	occupying the S3-S4 subsites on the SARS-CoV-2 PLpro with small molecule ligands can potentially inhibit the protease, deubiquitinating and deISGylating activities of the enzyme (PLpro). Molecular docking is used to investigate the binding properties of a selection of dietary compounds and naphthalene-based inhibitors to the binding site of GRL-0617. The structures of the SARS-CoV-2 and SARS-CoV PLpro in complex with interferon-stimulated gene 15 (ISG15) and lysine 48 (K48)-linked diubiquitin are utilised. To predict whether compounds could potentially interfere with the binding of these cellular modifiers, docking is conducted in the absence and presence of ISG15 and K48-linked diubiquitin	Severe acute respiratory syndrome coronavirus 2

Organism

Organism	UniProt	Comment	Textmining
Severe acute respiratory syndrome coronavirus 2	P0DTD1	SARS-CoV-2	-

Synonyms

Synonyms	Comment	Organism
PLpro	-	Severe acute respiratory syndrome coronavirus 2
SARS-CoV-2 papain-like protease	-	Severe acute respiratory syndrome coronavirus 2

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Release 2023.1 (January 2023)