Binding of Euplotes octocarinatus centrin to peptide from xeroderma pigmentosum group C protein (XPC)

Abstract

Trp is buried in the hydrophobic cavity, the peptide folds into an α-helix, and the interaction is enthalpically driven from ITC.

Endonuclease-like activity of the N-terminal domain of Euplotes octocarinatus centrin

“…22 centrin interacts directly with XP group C responsible gene product (XPC), and that centrin, in cooperation with human homologue of Rad23B (HR23B), stabilizes XPC, which stimulates NER activity in vitro. [23][24][25] Namely. They are localised appropriately to the sites of DNA damage by XPC and in turn control XPC stability and function.…”