Quantitative Analysis of the Substrate Specificity of Human Rhinovirus 3C Protease and Exploration of Its Substrate Recognition Mechanisms.
3C Viral Proteases
Amino Acid Sequence
Binding Sites
Cysteine Endopeptidases
/ chemistry
Gene Expression Regulation
Humans
Models, Molecular
Mutagenesis
Peptides
/ chemistry
Protein Binding
Protein Conformation
Rhinovirus
/ enzymology
Saccharomyces cerevisiae
/ genetics
Structure-Activity Relationship
Substrate Specificity
Temperature
Thermodynamics
Viral Proteins
/ chemistry
Journal
ACS chemical biology
ISSN: 1554-8937
Titre abrégé: ACS Chem Biol
Pays: United States
ID NLM: 101282906
Informations de publication
Date de publication:
17 01 2020
17 01 2020
Historique:
pubmed:
16
10
2019
medline:
14
1
2021
entrez:
16
10
2019
Statut:
ppublish
Résumé
Human rhinovirus 3C protease (HRV 3C-P) is a high-value commercial cysteine protease that could specifically recognize the short peptide sequence of LEVLFQ↓GP. In here, a strategy based on our previous Yeast Endoplasmic Reticulum Sequestration Screening (YESS) approach was developed in
Identifiants
pubmed: 31613083
doi: 10.1021/acschembio.9b00539
doi:
Substances chimiques
Peptides
0
Viral Proteins
0
Cysteine Endopeptidases
EC 3.4.22.-
3C Viral Proteases
EC 3.4.22.28
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM