Structural and molecular basis of interaction of HCV non-structural protein 5A with human casein kinase 1α and PKR.

ABSTRACT:

Background

Interaction of non-structural protein 5A (NS5A) of Hepatitis C virus (HCV) with human kinases namely, casein kinase 1α (ck1α) and protein kinase R (PKR) have different functional implications such as regulation of viral replication and evasion of interferon induced immune response respectively. Understanding the structural and molecular basis of interactions of the viral protein with two different human kinases can be useful in developing strategies for treatment against HCV.

Results

Serine 232 of NS5A is known to be phosphorylated by human ck1α. A structural model of NS5A peptide containing phosphoacceptor residue Serine 232 bound to ck1α has been generated using the known 3-D structures of kinase-peptide complexes. The substrate interacting residues in ck1α has

SUBMITTER: Sudha G 

PROVIDER: S-EPMC3534215 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature