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

Fernando Rodríguez-Castañeda, Nicolas Coudevylle, Stefan Becker, Nils Brose, Teresa Carlomagno, Christian Griesinger

Research output: Contribution to journalArticlepeer-review

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).

Original languageEnglish
Pages (from-to)45-8
Number of pages4
JournalBiomolecular NMR assignments
Volume4
Issue number1
DOIs
Publication statusPublished - Apr 2010

Keywords

  • Calmodulin/chemistry
  • Carbon Isotopes/chemistry
  • Hydrogen-Ion Concentration
  • Nerve Tissue Proteins/chemistry
  • Nitrogen/chemistry
  • Nitrogen Isotopes/chemistry
  • Nuclear Magnetic Resonance, Biomolecular
  • Recombinant Proteins/chemistry
  • Temperature

Fingerprint

Dive into the research topics of '1H, 13C and 15N resonance assignments of the Calmodulin-Munc13-1 peptide complex'. Together they form a unique fingerprint.

Cite this