Client Binding of Cdc37 Is Regulated Intramolecularly and Intermolecularly

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著者

    • Terasawa Kazuya TERASAWA Kazuya
    • Department of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems Biology, Graduate School of Science, The University of Tokyo
    • Shinozaki Fumika SHINOZAKI Fumika
    • Department of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems Biology, Graduate School of Science, The University of Tokyo
    • MINAMI Yasufumi
    • Department of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems Biology, Graduate School of Science, The University of Tokyo

抄録

Recently we showed that the glycine-rich loop in the N-terminal portion of protein kinases and the client-binding site of Cdc37 are both necessary for interaction between Cdc37 and protein kinases. We demonstrate here that the N-terminal portion of Cdc37, distinct from its client-binding site, interacts with the C-terminal portion of Raf-1. This interaction might expose the client-binding site of Cdc37. In addition, we provide evidence indicating that Cdc37 is monomeric in its physiological state, and that it becomes a dimer only when it is complexed with both Hsp90 and protein kinases.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(6), 1542-1546, 2006-06-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018530636
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    SHO
  • ISSN
    09168451
  • NDL 記事登録ID
    7959176
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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