Structural Insights into the Calmodulin−Munc13 Interaction Obtained by Cross-Linking and Mass Spectrometry

Munc13 proteins are essential regulators of synaptic vesicle priming and play a key role in adaptive synaptic plasticity phenomena. We recently identified and characterized the Ca2+-dependent interaction of Munc13 and calmodulin (CaM) as the molecular mechanism linking changes in residual Ca2+ conce...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biochemistry (Easton) 2009-06, Vol.48 (25), p.5908-5921
Hauptverfasser:	Dimova, Kalina, Kalkhof, Stefan, Pottratz, Ines, Ihling, Christian, Rodriguez-Castaneda, Fernando, Liepold, Thomas, Griesinger, Christian, Brose, Nils, Sinz, Andrea, Jahn, Olaf
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Calmodulin - chemistry Calmodulin - genetics Calmodulin - metabolism Cattle Chromatography, High Pressure Liquid Cross-Linking Reagents - chemistry Cross-Linking Reagents - metabolism Hydrophobic and Hydrophilic Interactions Molecular Sequence Data Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Photoaffinity Labels - chemical synthesis Photoaffinity Labels - metabolism Protein Binding - physiology Protein Structure, Tertiary Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!