Chemical shift assignments of calmodulin bound to the beta-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)

被引：5
|
作者：
Bej, Aritra [1 ]
Ames, James B. [1 ]
机构：
[1] Univ Calif Davis, Dept Chem, Davis, CA 95616 USA
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2022年 / 16卷 / 01期
关键词：
CaM; Calcium; CNGB1; Retina; Photoreceptor; NMR; SECONDARY STRUCTURE; MODULATION;
D O I：
10.1007/s12104-022-10072-9
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
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).
引用
收藏
页码：147 / 151
页数：5
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