Molecular Mechanisms of Functional Modulation of Transcriptional Coactivator PC4 via Phosphorylation on Its Intrinsically Disordered Region.

ABSTRACT: To investigate the effects of phosphorylation on the function of the human positive cofactor 4 (PC4), an enhanced molecular dynamics (MD) simulation was performed. The simulation system consists of the N-terminal intrinsic disordered region (IDR) of PC4 and a complex that comprises the C-terminal acidic activation domain of a herpes simplex virion protein 16 (VP16ad) and a homodimer of the C-terminal structured core domain of PC4 (PC4ctd). An earlier report of an experimental study reported that the PC4-VP16ad interaction is modulated by incremental phosphorylation of the IDR. That report also proposed a dynamic model where phosphorylated serine residues of a segment (SEAC) in the IDR contact positively charged residues (lysin and arginine) of another segment (K-rich) in the IDR. This cont

SUBMITTER: Xie Q 

PROVIDER: S-EPMC10134458 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature