Objectives and Methods

   We will determine how the DNA repair enzymes of the apurinic/apyrimidinic endonuclease (APE) family recognize the structure and dynamics of DNA damage sites resulting from low dose ionizing radiation (IR). Accurate crystal structures exist for the bacterial member of this family (Mol et al., 1995) and the human APE1 in complex with a synthetic, cleavable tetrahydrofuran analogue of an AP site (Mol et al., 2000). These crystal structures are used as the basis for homology modeling of other proteins of this family. We are running molecular dynamic simulations of wild type and mutant APE1 to analyze the flexibility of catalytically important residues and to predict alternative conformations of these proteins which might be important in recognition of damaged DNA sites. Blast and Psi-blast searching with the human APE1 sequence has revealed many related protein sequences, which are being used to locate structurally and functionally important residues. We further developing our expert system, MASIA (Hänggi and Braun, 1994; Zhu et al., 1999b), to identify motifs of conserved amino acids. These are used to identify other relatives of the APE family in the human genome family. The predictions we make will be tested in a unique complementation assay in APE deficient bacterial cells. We pursue the following specific aims: