Solution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plants

• Main Authors: Roy A., Lim L., Srivastava S., Lu Y., Song J.
• Other Authors: BIOLOGY (NU)
• Format: Article
• Published: Public Library of Science 2020
• Subjects: apigenin; aprotinin; catechin; curcumin; daidzein; flavonoid; isorhamnetin; luteolin; myricetin; natural product; NS2B NS3 protease; phenol; proteinase; quercetin; resveratrol; serine proteinase inhibitor; unclassified drug; biological product; buffer; NS2B protein, flavivirus; NS3 protein, flavivirus; RNA helicase; serine proteinase; solution and solubility; viral protein; Article; carboxy terminal sequence; catalysis; circular dichroism; drug identification; enzyme activity; enzyme conformation; enzyme inhibition; enzyme kinetics; fruit; IC50; molecular cloning; molecular docking; nonhuman; nuclear magnetic resonance spectroscopy; plasmid; protein expression; protein purification; protein secondary structure; protein tertiary structure; structure activity relation; vegetable; Zika virus; antagonists and inhibitors; binding site; biocatalysis; biophysics; chemistry; drug effects; edible plant; hydrogen bond; isolation and purification; kinetics; metabolism; molecular model; protein conformation; Binding Sites; Biocatalysis; Biological Products; Biophysical Phenomena; Buffers; Cloning, Molecular; Hydrogen Bonding; Kinetics; Models, Molecular; Plants, Edible; Protein Conformation; RNA Helicases; Serine Endopeptidases; Solutions; Viral Nonstructural Proteins; Zika Virus
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/165787
• Institution: National University of Singapore

10.1371/journal.pone.0180632