钙调蛋白与视紫红质环核苷酸门控通道（CNGB1）β亚基结合的化学位移分配。
Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1).
机构信息
Department of Chemistry, University of California, Davis, CA, 95616, USA.
出版信息
Biomol NMR Assign. 2022 Apr;16(1):147-151. doi: 10.1007/s12104-022-10072-9. Epub 2022 Feb 2.
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 Ca-bound CaM, which promotes Ca-induced inactivation of CNGA1/CNGB1 channels in retinal rods. We report complete NMR chemical shift assignments of Ca-saturated CaM bound to the CaM-binding domain of CNGB1 (BMRB no. 51222).
棒状细胞环核苷酸门控（CNG）通道由两个蛋白亚基（CNGA1 和 CNGB1）组成。钙调蛋白（CaM）与 CNGB1 的细胞质调节域结合，降低 CNG A1/CNGB1 通道的开放概率。牛 CNGB1 中的 CaM 结合位点（残基 679-702）与 Ca 结合的 CaM 紧密结合，促进视杆细胞中 CNG A1/CNGB1 通道的 Ca 诱导失活。我们报告了与 CNGB1 的 CaM 结合域结合的 Ca 饱和 CaM 的完整 NMR 化学位移赋值（BMRB 编号 51222）。
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