Evaluation of a single amino acid substitution at position 79 of human IFN-α2b in interferon-receptor assembly and activity.
Amino Acid Substitution
Animals
Antiviral Agents
/ chemistry
CHO Cells
Cell Proliferation
/ drug effects
Cricetulus
HeLa Cells
Humans
Interferon alpha-2
Interferon-alpha
/ chemistry
Molecular Docking Simulation
Protein Conformation
Protein Engineering
/ methods
Receptors, Interferon
/ metabolism
Recombinant Proteins
/ chemistry
Antiproliferative activity
IFN-α2b
antiviral activity
protein engineering
Journal
Preparative biochemistry & biotechnology
ISSN: 1532-2297
Titre abrégé: Prep Biochem Biotechnol
Pays: England
ID NLM: 9607037
Informations de publication
Date de publication:
2019
2019
Historique:
pubmed:
29
5
2019
medline:
9
8
2019
entrez:
29
5
2019
Statut:
ppublish
Résumé
Type I interferons (IFNs) are homologous cytokines that bind to a cell surface receptor and establish signaling pathways that motivate immune responses. The purpose of the current study is to assess the activity of a novel-engineered IFN-α2b. The crystallographic structure of IFN-α2b and its receptors was acquired from Protein Data Bank. Various amino acid substitutions were designed based on structural properties and other biological characteristics of residues to find the most effective amino acid on IFN affinity to advanced activities. The IFN-α2b mutants and receptors have been modeled and the interactions between two proteins have been studied as
Identifiants
pubmed: 31135267
doi: 10.1080/10826068.2019.1566143
doi:
Substances chimiques
Antiviral Agents
0
Interferon alpha-2
0
Interferon-alpha
0
Interferon-alpha2b
0
Receptors, Interferon
0
Recombinant Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM