{Reference Type}: Journal Article
{Title}: Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1).
{Author}: Bej A;Ames JB;
{Journal}: Biomol NMR Assign
{Volume}: 16
{Issue}: 1
{Year}: 04 2022
{Factor}: 0.731
{DOI}: 10.1007/s12104-022-10072-9
{Abstract}: Rod cyclic nucleotide-gated (CNG) channels are formed by two protein subunits (CNGA1 and CNGB1). Calmodulin (CaM) binds to the cytosolic regulatory domain of CNGB1 and decreases the open probability of CNGA1/CNGB1 channels. The CaM binding site within bovine CNGB1 (residues 679-702) binds tightly to Ca2+-bound CaM, which promotes Ca2+-induced inactivation of CNGA1/CNGB1 channels in retinal rods. We report complete NMR chemical shift assignments of Ca2+-saturated CaM bound to the CaM-binding domain of CNGB1 (BMRB no. 51222).