[HTML][HTML] Identification of the calmodulin binding domain of connexin 43
Calmodulin (CaM) has been implicated in mediating the Ca 2+-dependent regulation of gap
junctions. This report identifies a CaM-binding motif comprising residues 136–158 in the
intracellular loop of Cx43. A 23-mer peptide encompassing this CaM-binding motif was
shown to bind Ca 2+-CaM with 1: 1 stoichiometry by using various biophysical approaches,
including surface plasmon resonance, circular dichroism, fluorescence spectroscopy, and
NMR. Far UV circular dichroism studies indicated that the Cx43-derived peptide increased …
junctions. This report identifies a CaM-binding motif comprising residues 136–158 in the
intracellular loop of Cx43. A 23-mer peptide encompassing this CaM-binding motif was
shown to bind Ca 2+-CaM with 1: 1 stoichiometry by using various biophysical approaches,
including surface plasmon resonance, circular dichroism, fluorescence spectroscopy, and
NMR. Far UV circular dichroism studies indicated that the Cx43-derived peptide increased …