Structural Insight for Ca channel Regulation by Calmodulin

本研究的总体目的是了解钙结合蛋白钙调蛋白（Calmodulin, CaM）激活、抑制和调控钙通道的机制。主要的重点是确定无钙形式的apoam和通道IQ结构域复合物的结构。直到今天，我们有几个晶体，这些将需要检查再现性和它们的结构。对于Ca^<2+>和CaM通道相互作用的成像，我们成功地开发了结合Fura-2和FRET的新系统。利用该系统可以建立高保真的Ca^<2+>的体内滴定实验。我们希望这一方法将被广泛应用于生理科学领域，以揭示Ca^<2+>相关的分子动力学。

The overall aim of the proposed studies was to understand the mechanism of activation, inhibition and regulations of Ca channels by Calcium-binding protein Calmodulin (CaM). The primary focus was structural determination of the calcium free form apoCaM and Channel IQ domain complex. Until today, we have a couple of crystals, those will be needed to check reproducibility and their structure. For the imaging of Ca^<2+> and CaM- channel interaction, we have succeeded to develop new system combined with Fura-2 and FRET. By using this system we could establish Ca^<2+> titrative experiment in vivo with high fidelity. We hope that this approach will be often to use in the field wide range of the physiological science to reveal Ca^<2+> related molecular dynamics.