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The TRPV5/6 calcium channels contain multiple calmodulin binding sites with differential binding properties Kovalevskaya NV; Bokhovchuk FM; Vuister GWJ Struct Funct Genomics 2012[Jun]; 13 (2): 91-100The epithelial Ca(2+) channels TRPV5/6 (transient receptor potential vanilloid 5/6) are thoroughly regulated in order to fine-tune the amount of Ca(2+) reabsorption. Calmodulin has been shown to be involved into calcium-dependent inactivation of TRPV5/6 channels by binding directly to the distal C-terminal fragment of the channels (de Groot et al. in Mol Cell Biol 31:2845-2853, 12). Here, we investigate this binding in detail and find significant differences between TRPV5 and TRPV6. We also identify and characterize in vitro four other CaM binding fragments of TRPV5/6, which likely are also involved in TRPV5/6 channel regulation. The five CaM binding sites display diversity in binding modes, binding stoichiometries and binding affinities, which may fine-tune the response of the channels to varying Ca(2+)-concentrations.|Amino Acid Sequence[MESH]|Animals[MESH]|Binding Sites[MESH]|Calcium Channels/*chemistry[MESH]|Calcium/chemistry[MESH]|Calmodulin/*chemistry[MESH]|Cell Membrane/chemistry[MESH]|Escherichia coli/chemistry/genetics[MESH]|Humans[MESH]|Magnetic Resonance Spectroscopy[MESH]|Molecular Sequence Data[MESH]|Peptide Fragments/chemistry/isolation & purification[MESH]|Protein Binding[MESH]|Protein Interaction Mapping[MESH]|Recombinant Proteins/chemistry/genetics/isolation & purification[MESH]|TRPV Cation Channels/*chemistry[MESH]|Thermodynamics[MESH]|Tryptophan/chemistry[MESH]|Xenopus laevis/genetics[MESH] |
