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

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

Euplotes octocarinatus centrin (EoCen) is a member of the EF-hand superfamily of calcium-binding proteins, which refer to nucleotide excision repair (NER).

Modulation of XPC peptide on binding Tb3+ to Euplotes octocarinatus centrin

Metal ions weakly enhanced the affinity between EoCen and the XPC peptide, whereas the peptide remarkably modulated the binding of Tb3+ to the N-terminal domain of EoCen. Peptide binding resulted in the dissociation of EoCen aggregates, and the aggregation of EoCen induced by Tb3+ binding was inhibited.