生物物理
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
42 巻 , 2 号
通巻240号
選択された号の論文の9件中1~9を表示しています
巻頭言
解説
  • 和泉 義信
    原稿種別: 研究論文
    専門分野: 情報学
    2002 年 42 巻 2 号 p. 60-65
    発行日: 2002年
    公開日: 2002/04/09
    ジャーナル フリー
    Ca2+-free calmodulin (apocalmodulin) binds target proteins and alters their function. Apocalmodulin has roles in the cell that apparently do not require the ability to bind Ca2+ at all, and these roles appear to be essential for cell's metabolism. Small-angle X-ray scattering (SAXS) results indicate that the overall conformation of apocalmodulin remains unchanged, but the conformation for the C-domain changes from the closed to semi-open conformation upon binding the target proteins. The conformational change would be induced by electrostatic interactions and subsequent van der Waals interactions and it can cause changes in the Ca2+ affinity of the apocalmodulin-target protein complex. An analysis of residue pairs between calmodulin and target peptides suggests that apocalmodulin recognizes Ca2+-dependent calmodulin binding proteins, utilizing a new motif different from IQ motif.
総説
トピックス
実験技術
feedback
Top