1H, 13C and 15N resonance assignments of the Calmodulin-Munc13-1 peptide complex

被引：4

作者：

Rodriguez-Castaneda, Fernando ^{[1
]}

Coudevylle, Nicolas ^{[1
]}

Becker, Stefan ^{[1
]}

Brose, Nils ^{[2
]}

Carlomagno, Teresa ^{[1
]}

Griesinger, Christian ^{[1
]}

机构：

[1] Max Planck Inst Biophys Chem, NMR Based Struct Biol Dept, D-37077 Gottingen, Germany

[2] Max Planck Inst Expt Med, Dept Mol Neurobiol, D-37075 Gottingen, Germany

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2010年 / 4卷 / 01期

关键词：

Calcium; Calmodulin; Munc13; Neurotransmitter release; Synaptic plasticity; Phorbol esters and vesicle priming; CAENORHABDITIS-ELEGANS; RECOGNITION; PROTEINS; UNC-13; FORM;

D O I：

10.1007/s12104-009-9204-2

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Ca2+-Calmodulin binding to the variable N-terminal region of the diacylglycerol/phorbol ester-binding UNC13/Munc13 family of proteins modulates the short-term synaptic plasticity characteristics in neurons. Here, we report the sequential backbone and side chain resonance assignment of the Ca2+-Calmodulin/Munc13-1(458-492) peptide complex at pH 6.8 and 35A degrees C (BMRB No. 15470).

引用

页码：45 / 48

页数：4

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