Mechanism for the Transport of ABC Transporters by Experimental and Simulation Studies

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  • FURUTA Tadaomi
    Graduate School of Bioscience & Biotechnology, Tokyo Institute of Technology
  • YAMAGUCHI Tomohiro
    Graduate School of Pharmaceutical Sciences, Kyoto University
  • KATO Hiroaki
    Graduate School of Pharmaceutical Sciences, Kyoto University
  • SAKURAI Minoru
    Center for Biological Resources & Informatics, Tokyo Institute of Technology

Bibliographic Information

Other Title
  • 実験とシミュレーションを用いたABCトランスポーターによる物質輸送の機構解明
  • ジッケン ト シミュレーション オ モチイタ ABC トランスポーター ニ ヨル ブッシツ ユソウ ノ キコウ カイメイ

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Abstract

ATP-binding cassette (ABC) transporters constitute one of the largest superfamilies of membrane proteins that translocate variable substrates through the transmembrane domains (TMDs) powered by the ATP-driven nucleotide-binding domain (NBDs) engines. The coupling helices (CHs) located at the NBD-TMD interfaces play important roles in the structural transition between the inward- and outward-facing conformations. Here, we review our recent studies on the roles of CHs and the effects of ATP and substrates in the functional dynamics of ABC transporters.

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 56 (1), 005-008, 2016

    The Biophysical Society of Japan General Incorporated Association

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