The group works with the structural biology of DNA repair with the aim to understand the damage recognition mechanisms and enzymatic catalysis at the atomic level. The major focus is on base excision repair and DNA glycosylases, which are involved in detection and elimination of chemically modified nucleotides with a mutagenic potential. Major methods include X-ray crystallography, protein-ligand interaction studies, single-molecule imaging of DNA scanning and inhibitor screening. The human DNA glycosylases are also potential drug targets in cancer therapy, and we also use structure-based methods to identify possible inhibitors that may work as adjuvants in cancer therapy. The group is also responsible for the daily operation of the Helse Sør-Øst regional core facility for structural biology. The core facility has been involved in projects related to a diverse range of topics such as immunology, metabolic disorders (cholesterol metabolism, MSUD, vitamin B12-metabolism), glycosylation defects, various cancer-related targets, protein kinases, DNA/RNA processing.
Peptides containing the PCNA interacting motif APIM bind to the β-clamp and inhibit bacterial growth and mutagenesis
Nucleic Acids Res (in press)
An intact C-terminal end of albumin is required for its long half-life in humans
Commun Biol, 3 (1), 181
Author Correction: Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus
Sci Rep, 10 (1), 6287