Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair

NMR spectroscopy and molecular modeling are used to characterize the solution Ca(super 2+)-dependent structural and molecular features of the C-terminal domain of centrin (C-HsCen2) in complex with a peptide from the xeroderma pigmentosum group C protein ( Pl-XPC). Investigation of the centrin interactions show that the N-terminal domain of the protein is not involved in the complex formation and is structurally independent from the peptide-bound C-terminal domain.