About: Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C‐like protease (SARS‐CoV 3CL (pro)) from its polyproteins

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About: Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C‐like protease (SARS‐CoV 3CL (pro)) from its polyproteins Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C‐like protease (SARS‐CoV 3CL (pro)) from its polyproteins
Creator	Kim, Yong-Tae Muramatsu, Tomonari Nishii, Wataru Shirouzu, Mikako Terada, Takaho Yokoyama, Shigeyuki
source	Medline; PMC
abstract	Like many other RNA viruses, severe acute respiratory syndrome coronavirus (SARS‐CoV) produces polyproteins containing several non‐structural proteins, which are then processed by the viral proteases. These proteases often exist within the polyproteins, and are excised by their own proteolytic activity (‘autoprocessing’). It is important to investigate the autoprocessing mechanism of these proteases from the point of view of anti‐SARS‐CoV drug design. In this paper, we describe a new method for investigating the autoprocessing mechanism of the main protease (M (pro)), which is also called the 3C‐like protease (3CL (pro)). Using our method, we measured the activities, under the same conditions, of the mature form and pro‐forms with the N‐terminal pro‐sequence, the C‐terminal pro‐sequence or both pro‐sequences, toward the pro‐form with both N‐ and C‐terminal pro‐sequences. The data indicate that the pro‐forms of the enzyme have proteolytic activity, and are stimulated by the same proteolytic activity. The stimulation occurs in two steps, with approximately eightfold stimulation by N‐terminal cleavage, approximately fourfold stimulation by C‐terminal cleavage, and 23‐fold stimulation by the cleavage of both termini, compared to the pro‐form with both the N‐ and C‐terminal pro‐sequences. Such cleavage mainly occurs in a trans manner; i.e. the pro‐form dimer cleaves the monomeric form. The stimulation by N‐terminal pro‐sequence removal is due to the cis (intra‐dimer and inter‐protomer) effect of formation of the new N‐terminus, whereas that by C‐terminal cleavage is due to removal of its trans (inter‐dimer) inhibitory effect. A numerical simulation of the maturation pathway is presented.
has issue date	2013-03-27(xsd:dateTime)
bibo:doi	10.1111/febs.12222
bibo:pmid	23452147
has license	no-cc
sha1sum (hex)	827103fa191ba00e6b77c07e58b39204bf13fd22
schema:url	https://doi.org/10.1111/febs.12222
resource representing a document's title	Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C‐like protease (SARS‐CoV 3CL (pro)) from its polyproteins
has PubMed Central identifier	PMC7164132
has PubMed identifier	23452147
schema:publication	FEBS J
resource representing a document's body	covid:827103fa191ba00e6b77c07e58b39204bf13fd22#body_text
is schema:about of	named entity 'removal' named entity 'excised' named entity 'SARS-CoV' named entity 'activity' named entity 'cis' named entity 'proteolytic' named entity 'pro' named entity 'SARS-CoV' named entity 'stimulation' named entity 'cleavage' named entity 'mature' named entity 'cleavage' named entity 'pro' named entity 'stimulation' named entity 'drug design' named entity 'proteases' named entity 'cis' named entity 'pro-form' named entity 'pro-form' named entity 'C-terminal' named entity 'numerical simulation' named entity 'C-terminal' named entity 'proteolytic activity' named entity 'trans' named entity 'N-terminal' named entity 'SARS-CoV' named entity 'dimer' named entity 'protomer' named entity 'protomer' named entity 'C-terminal' named entity 'pro-form' named entity 'polyprotein' named entity 'wild-type' named entity 'virion' named entity 'enzyme' named entity 'substrate' named entity 'E. coli' named entity 'assay' named entity 'C-terminal' named entity 'substrate' named entity 'World Health Organization' named entity 'Darmstadt' named entity 'proximal' named entity 'polyprotein' named entity 'substrate' named entity 'active site' named entity 'nsp4' named entity 'amino acids' named entity 'GFP' named entity 'membrane topology' named entity 'E. coli' named entity 'cis' named entity 'dimeric structure' named entity 'N-termini' named entity 'protomers' named entity 'amino acid residues' named entity 'BSA' named entity 'Taipei' named entity 'substrate' named entity 'amino acid residues' named entity 'dimer' named entity 'protomer' named entity 'protein' named entity 'substrate' named entity 'N-terminal' named entity 'pro-form' named entity 'pro-form' named entity 'proforms' named entity 'assay' named entity 'N-terminal' named entity 'cell-free protein synthesis' named entity 'substrate' named entity 'Coomassie Brilliant Blue G-250' named entity 'substrate' named entity 'dimer' named entity 'moiety'

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