钙调蛋白与视网膜环核苷酸门控通道（CNGB1）β亚基 C 端结合位点（残基 1120-1147）的化学位移分配。
Chemical shift assignments of calmodulin bound to a C-terminal site (residues 1120-1147) in 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 Oct;16(2):337-341. doi: 10.1007/s12104-022-10101-7. Epub 2022 Aug 20.
Retinal cyclic nucleotide-gated (CNG) channels consist of two protein subunits (CNGA1 and CNGB1). Calmodulin (CaM) binds to two separate sites within the cytosolic region of CNGB1: CaM binding to an N-terminal site (human CNGB1 residues 565-587, called CaM1) decreases the open probability of CNG channels at elevated Ca levels in dark-adapted photoreceptors, whereas CaM binding to a separate C-terminal site (CNGB1 residues 1120-1147, called CaM2) may increase channel open probability in light activated photoreceptors. We recently reported NMR chemical shift assignments of Ca-saturated CaM bound to the CaM1 site of CNGB1 (BMRB no. 51222). Here, we report complete NMR chemical shift assignments of Ca-saturated CaM bound to the C-terminal CaM2 site of CNGB1 (BMRB no. 51447).
视网膜环核苷酸门控 (CNG) 通道由两个蛋白亚基 (CNGA1 和 CNGB1) 组成。钙调蛋白 (CaM) 结合到 CNGB1 细胞溶质区域内的两个不同位点：CaM 结合到 N 端位点 (人 CNGB1 残基 565-587，称为 CaM1)，在黑暗适应的光感受器中，在升高的 Ca 水平下降低 CNG 通道的开放概率，而 CaM 结合到一个单独的 C 端位点 (CNGB1 残基 1120-1147，称为 CaM2)，可能会增加光激活的光感受器中通道的开放概率。我们最近报道了 Ca 饱和的 CaM 与 CNGB1 的 CaM1 位点结合的 NMR 化学位移赋值 (BMRB 编号 51222)。在这里，我们报告了 Ca 饱和的 CaM 与 CNGB1 的 C 端 CaM2 位点结合的完整 NMR 化学位移赋值 (BMRB 编号 51447)。
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