The interaction between calmodulin (CaM) and Al3+was studied by spectroscopic methods. Heteronuclear two-dimensional NMR data indicated that peaks related to the both lobes and middle of the central helix of CaM are largely affected by Al3+. But chemical shift perturbation suggested that overall conformation of Ca2+-loaded CaM is not changed by Al3+binding. It is thought that Al3+interaction to the middle of the central helix is a key for the property of CaM's target recognition. If the structure and/or flexibility of the central helix are/is changed by Al3+, target affinity to CaM must be influenced by Al3+. Thus, we performed surface plasmon resonance experiments to observe the effect of Al3+on the target recognition by CaM. The data clearly indicated that target affinity to CaM is reduced by addition of Al3+. All the results presented here support a hypothesis that Al3+may affect on the Ca2+signaling pathway in cells. © 2005 Elsevier Inc. All rights reserved.
Kurita, H., Nakatomi, A., Shimahara, H., Yazawa, M., & Ohki, S. Y. (2005). Al3+ interaction sites of calmodulin and the Al3+ effect on target binding of calmodulin. Biochemical and Biophysical Research Communications, 333(4), 1060–1065. https://doi.org/10.1016/j.bbrc.2005.06.016