Computational study on the inhibitor binding mode and allosteric regulation mechanism in hepatitis C virus NS3/4A protein.
HCV NS3/4A protein is an attractive therapeutic target responsible for harboring serine protease and RNA helicase activities during the viral replication. Small molecules binding at the interface between the protease and helicase domains can stabilize the closed conformation of the protein and thus...
Guardado en:
Autores principales: | Weiwei Xue, Ying Yang, Xiaoting Wang, Huanxiang Liu, Xiaojun Yao |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2014
|
Materias: | |
Acceso en línea: | https://doaj.org/article/02d46c9c0ec640b5bcd27181f8af2e37 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Molecular modeling study on the allosteric inhibition mechanism of HIV-1 integrase by LEDGF/p75 binding site inhibitors.
por: Weiwei Xue, et al.
Publicado: (2014) -
Inhibitor binding mode and allosteric regulation of Na + -glucose symporters
por: Paola Bisignano, et al.
Publicado: (2018) -
Quantifying the Evolutionary Constraints and Potential of Hepatitis C Virus NS5A Protein
por: Lei Dai, et al.
Publicado: (2021) -
NS2 protein of hepatitis C virus interacts with structural and non-structural proteins towards virus assembly.
por: Costin-Ioan Popescu, et al.
Publicado: (2011) -
Structural and regulatory elements of HCV NS5B polymerase--β-loop and C-terminal tail--are required for activity of allosteric thumb site II inhibitors.
por: Sarah E Boyce, et al.
Publicado: (2014)