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Updated: May 15, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Resonance assignments and secondary structure of calmodulin in complex with its target sequence in rat olfactory
Deli Irene1, Fu-Hsing Sung, Jian-Wen Huang
1Department of Chemistry, National Dong Hwa University, Shoufeng, Hualien, 974, Taiwan, ROC.
Abstract:
Calmodulin (CaM), the primary receptor for intracellular Ca(2+), regulates a large number of key enzymes and controls a wide spectrum of important biological responses. Olfactory cyclic nucleotide-gated ion channels (OLF channels) mediate olfactory transduction in olfactory receptor neurons. The opening of OLF leads to a rise in cytosolic concentration of Ca(2+), upon binding to Ca(2+), CaM disrupts the open conformation by binding to the CaM-binding domain in the N-terminal region and triggers the close mechanism. In order to unravel the regulatory role of CaM from structural point of view, NMR techniques were used to characterize the structure of CaM in association with the CaM binding domain of rat OLF channel (OLFp, 28 residues). Our data indicated that two distinct CaM/OLFp complexes existed simultaneously with stable structures that were not inter-exchangeable within the NMR time scale. Here, we report the full backbone and side chain resonance assignments of these two complexes of CaM/OLFp.
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