ヒト由来ポリADP-リボｰスポリメラｰゼの立体構造解析 : 阻害剤結合による活性部位の構造変化

スポンサーリンク

概要

• 論文の詳細を見る

• The crystal structure of the catalytic domain of human recombinant poly (ADP-ribose) polymerase (PARP) complexed with a potent inhibitor, FR257517, was solved at 3.0 Å resolution. The fluorophenyl part of the inhibitor induces an amazing structural change in the active site of PARP by motion of the side chain of the amino acid, Arg878, which forms the bottom of the active site. Consequently, a corn-shape hydrophobic subsite, which consists of the side chains of Leu769, Ile879, Pro881, and the methylene chain of Arg878, newly emerges from the well-known active site. This observation should provide a new concept in PARP inhibitor design.

• 日本結晶学会の論文
• 2004-12-24

著者

• 木下 誉富

  藤沢薬品工業(株)探索研究所

関連論文

• ヒト由来ポリADP-リボｰスポリメラｰゼの立体構造解析 : 阻害剤結合による活性部位の構造変化
• タンパクX線結晶解析を用いる創薬

スポンサーリンク