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University of Connecticut Health Center - Know Better Care The Gregory P. Mullen NMR Structural Biology Facility & Biophysical Core Facility

N-terminal DNA-binding domain of DNA polymerase β

Human DNA is insulted by 10,000 to 1 million damage events per living cell per day. Inefficient repair of DNA damage leads to aging, cancer, and other diseases. DNA polymerase β functions in the base excision repair pathway by filling in short patches of damaged DNA and by catalyzing the removal of deoxyribose 5'-phosphate (dRP lyase) from the 5' side of damaged DNA. The N-terminal domain, shown here, binds gapped dsDNA and ssDNA and provides dRP lyase activity.

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Maciejewski, M.W., Liu, D-J., Prasad, R., Wilson, S.H. and Mullen, G.P. (2000) Backbone dynamics and refined solution structure of the N-terminal domain of DNA polymerase β. Correlation with DNA binding and dRP lyase activity. Journal of Molecular Biology 296, 229-253.

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