Domain Mobility in the ORF2p Complex Revealed by Molecular Dynamics Simulations and Big Data Analysis.

ABSTRACT: ORF2p (open reading frame 2 protein) is a multifunctional multidomain enzyme that demonstrates both reverse transcriptase and endonuclease activities and is associated with the pathophysiology of cancer. The 3D structure of the entire seven-domain ORF2p complex was revealed with the recent achievements in structural studies. The different arrangements of the CTD (carboxy-terminal domain) and tower domains were identified as the "closed-ring" and "open-ring" conformations, which differed by the hairpin position of the tower domain, but the structural diversity of these complexes has the potential to be more extensive. To study this, we performed sub-microsecond all-atom molecular dynamics simulations of the entire ORF2p complex with different starting configurations. The obtained molecular

SUBMITTER: Kulakova AM 

PROVIDER: S-EPMC11719894 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature