1H, 13C and 15N resonance assignments of the Calmodulin-Munc13-1 peptide complex.
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).
Rodríguez-Castañeda
Fernando
F
NMR-Based Structural Biology Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Coudevylle
Nicolas
N
Becker
Stefan
S
Brose
Nils
N
Carlomagno
Teresa
T
Griesinger
Christian
C
D002147:Calmodulin / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D009584:Nitrogen / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D011994:Recombinant Proteins / Q000737:chemistry; D013696:Temperature
D002147:Calmodulin; D002247:Carbon Isotopes; D009419:Nerve Tissue Proteins; D009587:Nitrogen Isotopes; D011994:Recombinant Proteins; D009584:Nitrogen