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Chemical shift assignments of a calmodulin intermediate with two Ca2+ bound in complex with the IQ-motif of voltage-gated Ca2+ channels (CaV1.2).
Biomolecular NMR Assignments ( IF 0.8 ) Pub Date : 2019-02-20 , DOI: 10.1007/s12104-019-09883-0
Ian Salveson 1 , David E Anderson 1 , Johannes W Hell 2 , James B Ames 1
Affiliation  

Calcium-dependent inactivation (CDI) of neuronal voltage-gated Ca2+ channels (CaV1.2) is important for synaptic plasticity, which is associated with learning and memory. The Ca2+-dependent binding of calmodulin (CaM) to CaV1.2 is essential for CDI. Here we report NMR assignments for a CaM mutant (D21A/D23A/D25A/E32Q/D57A/D59A/N61A/E68Q, called CaMEF12) that contains two Ca2+ bound at the third and fourth EF-hands (EF3 and EF4) and is bound to the IQ-motif (residues 1644–1665) from CaV1.2 (BMRB accession no. 27692).

中文翻译:

钙调素中间体的化学位移分配与两个 Ca2+ 结合,与电压门控 Ca2+ 通道 (CaV1.2) 的 IQ 基序复合。

神经元电压门控 Ca 2+通道 (Ca V 1.2) 的钙依赖性失活 (CDI) 对于与学习和记忆相关的突触可塑性很重要。钙调蛋白 (CaM) 与 Ca V 1.2的 Ca 2+依赖性结合对于 CDI 至关重要。在这里,我们报告了 CaM 突变体(D21A/D23A/D25A/E32Q/D57A/D59A/N61A/E68Q,称为 CaM EF12)的NMR 分配,其中包含在第三和第四个 EF 手(EF3 和 EF4)处结合的两个 Ca 2+并与 Ca V 1.2(BMRB 登录号 27692)的 IQ 基序(残基 1644-1665)结合。
更新日期:2019-02-20
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