title: Resonance assignments and secondary structure of calmodulin in complex with its target sequence in rat olfactory cyclic nucleotide-gated ion channel.
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.
authors: Department of Chemistry, National Dong Hwa University, Shoufeng, Hualien, 974, Taiwan, ROC.
authors: Deli
authors: D
authors: Irene
authors: Fu-Hsing
authors: FH
authors: Sung
authors: Jian-Wen
authors: JW
authors: Huang
authors: Ta-Hsien
authors: TH
authors: Lin
authors: Yi-chen
authors: YC
authors: Chen
authors: Chia-Lin
authors: CL
authors: Chyan
mesh_terms: D000818:Animals; D002147:Calmodulin / Q000737:chemistry*; D054815:Cyclic Nucleotide-Gated Cation Channels / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D009830:Olfactory Bulb / Q000378:metabolism*; D017433:Protein Structure, Secondary; D051381:Rats
chemical_list: D002147:Calmodulin; D054815:Cyclic Nucleotide-Gated Cation Channels