Talk:SARS-CoV-2 Papain-Like protease (PLpro)
From Proteopedia
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== Introduction == | == Introduction == | ||
Papain-like protease (PLpro) from SARS-CoV-2 is a 315 amino acids long cysteine protease is found in the large multi-domain membrane-bound non-structural protein 3 (nsp3)(1945 residues) between the SARS domain (SUD/HVR) and a nucleic acid-binding domain (NAD) (Frick et al, 2020, OSIPIUK et al., 2021). It has a high percentage of cysteine residues (3.5%) (OSIPIUK et al., 2021). | Papain-like protease (PLpro) from SARS-CoV-2 is a 315 amino acids long cysteine protease is found in the large multi-domain membrane-bound non-structural protein 3 (nsp3)(1945 residues) between the SARS domain (SUD/HVR) and a nucleic acid-binding domain (NAD) (Frick et al, 2020, OSIPIUK et al., 2021). It has a high percentage of cysteine residues (3.5%) (OSIPIUK et al., 2021). | ||
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PLpro active site is represented by C111S and contains the canonical protease catalytic triad composed by Cys111, His272, and Asp286. Differing from the dyad of Mpro, composed of Cys145 and His41. For PLpro Cys111 acts as a nucleophile and Asp286 promotes deprotonation of His272 (OSIPIUK et al., 2021). The residue C11 is 3.6 Å from H272 and the hydrogen bond donated by H272 to D286 has a 3.0 Å distance. (GAO et al., 2021) | PLpro active site is represented by C111S and contains the canonical protease catalytic triad composed by Cys111, His272, and Asp286. Differing from the dyad of Mpro, composed of Cys145 and His41. For PLpro Cys111 acts as a nucleophile and Asp286 promotes deprotonation of His272 (OSIPIUK et al., 2021). The residue C11 is 3.6 Å from H272 and the hydrogen bond donated by H272 to D286 has a 3.0 Å distance. (GAO et al., 2021) | ||
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Revision as of 21:55, 12 December 2021
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Introduction
Papain-like protease (PLpro) from SARS-CoV-2 is a 315 amino acids long cysteine protease is found in the large multi-domain membrane-bound non-structural protein 3 (nsp3)(1945 residues) between the SARS domain (SUD/HVR) and a nucleic acid-binding domain (NAD) (Frick et al, 2020, OSIPIUK et al., 2021). It has a high percentage of cysteine residues (3.5%) (OSIPIUK et al., 2021).
SARS-CoV-2 polyprotein
The first SARS-CoV-2 open reading frame (ORF) codes for one large polyprotein, 1ab (7096 aminoacids) or 1a (4405 amino acids) built by fifteen non-coding proteins including the two proteases responsible to cleave the polyprotein: Main protease (Mpro or 3Cl-pro) and Papain-Like protease (OSIPIUK et al., 2021).
Structure
PLpro active site is represented by C111S and contains the canonical protease catalytic triad composed by Cys111, His272, and Asp286. Differing from the dyad of Mpro, composed of Cys145 and His41. For PLpro Cys111 acts as a nucleophile and Asp286 promotes deprotonation of His272 (OSIPIUK et al., 2021). The residue C11 is 3.6 Å from H272 and the hydrogen bond donated by H272 to D286 has a 3.0 Å distance. (GAO et al., 2021)
