Three-Dimensional Structural Model Analysis of the Binding Site of Lithocholic Acid, an Inhibitor of DNA Polymerase .BETA. and DNA Topoisomerase II.

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概要

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• The molecular action of lithocholic acid (LCA), a selective inhibitor of mammalian DNA polymerase β (pol β), was investigated. We found that LCA could also strongly inhibit the activity of human DNA topoisomerase II (topo II). No other DNA metabolic enzymes tested were affected by LCA. Therefore, LCA should be classified as an inhibitor of both pol β and topo II. Here, we report the molecular interaction of LCA with pol β and topo II. By three-dimensional structural model analysis and by comparison with the spatial positioning of specific amino acids binding to LCA on pol β(Lys60, Leu77, and Thr79), we obtained supplementary information that allowed us to build a structural model of topo II. Modeling analysis revealed that the LCA-interaction interface in both enzymes has a pocket comprised of three amino acids in common, which binds to the LCA molecule. In topo II, the three amino acid residues were Lys720, Leu760, and Thr791. These results suggested that the LCA binding domains of pol β and topo II are three-dimensionally very similar.

• 社団法人 日本生化学会の論文

著者

• YOSHIDA Hiromi

  Laboratory of Food & Nutritional Sciences, Department of Nutritional Science, Kobe-Gakuin University

• Iida Akira

  Graduate School Of Pharmaceutical Sciences Kyoto University

• Sugawara Fumio

  Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University

• Sakaguchi Kengo

  Department Of Applied Biological Science Faculty Of Science And Technology Science University Of Tok

• Kasai Nobuyuki

  Department Of Agrobioscience Graduate School Of Agricultural Science Kobe University

• Mizushina Yoshiyuki

  Laboratofy of Food & Nutritional Sciences, Department al Nutritional Science, and High Technology Research Center, Kobe-Colmar University

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