Resonance assignments and secondary structure of calmodulin in complex with its target sequence in rat olfactory cyclic nucleotide-gated ion channel

Deli Irene, Fu Hsing Sung, Jian Wen Huang, Ta Hsien Lin, Yi Chen Chen, Chia Lin Chyan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Calmodulin (CaM), the primary receptor for intracellular Ca2+, regulates a large number of key enzymes and controls a wide spectrum of important biological responses. Olfactory cyclic nucleotide-gated ion channels (OLF channels) mediate olfactory transduction in olfactory receptor neurons. The opening of OLF leads to a rise in cytosolic concentration of Ca2+, upon binding to Ca2+, CaM disrupts the open conformation by binding to the CaM-binding domain in the N-terminal region and triggers the close mechanism. In order to unravel the regulatory role of CaM from structural point of view, NMR techniques were used to characterize the structure of CaM in association with the CaM binding domain of rat OLF channel (OLFp, 28 residues). Our data indicated that two distinct CaM/OLFp complexes existed simultaneously with stable structures that were not inter-exchangeable within the NMR time scale. Here, we report the full backbone and side chain resonance assignments of these two complexes of CaM/OLFp.

Original languageEnglish
Pages (from-to)97-102
Number of pages6
JournalBiomolecular NMR Assignments
Volume8
Issue number1
DOIs
StatePublished - Apr 2014

Keywords

  • Calmodulin
  • Olfactory nucleotide-gated ion channel
  • Protein NMR
  • Recognition

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