钙调蛋白-Munc13-1肽复合物的1H、13C和15N共振归属
1H, 13C and 15N resonance assignments of the Calmodulin-Munc13-1 peptide complex.
作者信息
Rodríguez-Castañeda Fernando, Coudevylle Nicolas, Becker Stefan, Brose Nils, Carlomagno Teresa, Griesinger Christian
机构信息
NMR-Based Structural Biology Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
出版信息
Biomol NMR Assign. 2010 Apr;4(1):45-8. doi: 10.1007/s12104-009-9204-2. Epub 2009 Dec 15.
Abstract
Ca(2+)-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 Ca(2+)-Calmodulin/Munc13-1(458-492) peptide complex at pH 6.8 and 35 degrees C (BMRB No. 15470).
摘要
钙离子-钙调蛋白与二酰基甘油/佛波酯结合的UNC13/Munc13蛋白家族可变N端区域的结合调节神经元中的短期突触可塑性特征。在此，我们报道了在pH 6.8和35摄氏度下（BMRB编号15470）钙离子-钙调蛋白/Munc13-1(458 - 492)肽复合物的主链和侧链共振顺序归属。
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