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Literature summary for 3.4.22.B80 extracted from

  • Wu, C.; Liu, Y.; Yang, Y.; Zhang, P.; Zhong, W.; Wang, Y.; Wang, Q.; Xu, Y.; Li, M.; Li, X.; Zheng, M.; Chen, L.; Li, H.
    Analysis of therapeutic targets for SARS-CoV-2 and discovery of potential drugs by computational methods (2020), Acta Pharm. Sin. B, 10, 766-788 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
drug development SARS-CoV-2 papain like protease is an important anti-virus drug target protein for the development of small-molecule inhibitors Severe acute respiratory syndrome coronavirus 2

Inhibitors

Inhibitors Comment Organism Structure
additional information discovery of potential drugs by computational methods. Screening results show that a series of anti-virus drugs (ribavirin, valganciclovir and thymidine), anti-bacterial drugs (chloramphenicol, cefamandole and tigecycline), muscle relaxant drug (chlorphenesin carbamate), anti-tussive drug (levodropropizine) may have high binding affinity to PLpro. The natural products, such as platycodin D from Platycodon grandiflorus, baicalin from Scutellaria baicalensis, sugetriol-3,9-diacetate from Cyperus rotundus, phaitanthrin D and 2,2-di (3-indolyl)-3-indolone from Isatis indigotica, catechin compounds ((e)-epigallocatechin gallate and 2-(3,4-dihydroxyphenyl)-2-[[2-(3,4-dihydroxyphenyl)-3,4-dihydro-5,7-dihydroxy-2H-1-benzopyran-3-yl]oxy]-3,4-dihydro-2H-1-benzopyran-3,4,5,7-tetrol) exhibit high binding affinity to PLpro protein, suggesting the potential utility of these compounds in the treatment of SARS-CoV-2. Anti-viral drug ribavirin is predicted to bind to PLpro with low binding energy. From generated docking model, ribavirin is bound in the active site of the enzyme as reported SARS-PLpro inhibitors. Hydrogen bonds are predicted between Gly164, Gln270, Tyr274, Asp303 and the compound. The strong hydrogen bonding and hydrophobic interaction between ribavirin with the enzyme imply it may be a potent PLpro inhibitor Severe acute respiratory syndrome coronavirus 2

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome coronavirus 2
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 SARS-CoV-2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SARS-CoV-2 large replicase polyprotein + H2O the enzyme (PLpro) cleaves three sites at 181-/-182, 818-/-819, and 2763-/-2764 at the N-terminus of SARS-CoV-2 large replicase polyprotein (SARS-CoV-2 PP1ab) Severe acute respiratory syndrome coronavirus 2 ?
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 ?

Synonyms

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

General Information

General Information Comment Organism
drug target important anti-virus drug target protein Severe acute respiratory syndrome coronavirus 2
physiological function the enzyme is responsible for the cleavages of N-terminus of the replicase polyprotein to release Nsp1, Nsp2 and Nsp3, which is essential for correcting virus replication. It is an indispensable enzyme in the process of coronavirus replication and infection of the host Severe acute respiratory syndrome coronavirus 2