85(P-87) DNAポリメラーゼβおよびDNAトポイソメラーゼII阻害物質を用いた両酵素の立体構造相関(ポスター発表の部)

概要

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There is no enzymatic similarity between DNA polymerase and DNA topoisomerase, although they are critical to many cellular processes such as DNA replication, repair and recombination, and subsequently, may act in harmony with each other. Long chain fatty acids selectively bind to DNA binding sites of DNA polymerase β and DNA topoisomerase II, and inhibit their activities, although the amino acid sequences of these enzymes are markedly different from each other. Computer modeling analysis revealed that the fatty acid interaction interface in both enzymes has a four amino acid group in common forming a pocket, which binds to the fatty acid molecule. The four amino acid residues were Thr596, His735, Leu741 and Lys983 for DNA topoisomerase II, corresponding to Thr79, His51, Leu11 and Lys35 for DNA polymerase β. Using three-dimensional structure model analysis, we determined the spatial positioning of specific amino acids binding to the fatty acids in DNA topoisomerase II, and subsequently obtained supplementary information to build the structural model.
天然有機化合物討論会の論文
2000-10-01