Client Binding of Cdc37 Is Regulated Intramolecularly and Intermolecularly
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概要
- 論文の詳細を見る
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.
- 社団法人 日本農芸化学会の論文
- 2006-06-23
著者
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MINAMI Michiko
Department of Natural and Environmental Science, Faculty of Education, Tokyo Gakugei University
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Shinozaki Fumika
Department Of Biophysics And Biochemistry And Undergraduate Program For Bioinformatics And Systems B
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Minami Michiko
Department Of Natural And Environmental Science Faculty Of Education Tokyo Gakugei University
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TERASAWA Kazuya
Department of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems
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MINAMI Yasufumi
Department of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems
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Minami Yasufumi
Department Of Biophysics And Biochemistry And Undergraduate Program For Bioinformatics And Systems B
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Terasawa Kazuya
Department Of Biophysics And Biochemistry And Undergraduate Program For Bioinformatics And Systems B
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