Journal of Biomolecular NMR

, Volume 31, Issue 3, pp 185–199

Structure of calmodulin complexed with an olfactory CNG channelfragment and role of the central linker: Residual dipolar couplingsto evaluate calmodulin binding modes outside the kinase family

  • Gian Marco Contessa
  • Maria Orsale
  • Sonia Melino
  • Vincent Torre
  • Maurizio Paci
  • Alessandro Desideri
  • Daniel O. Cicero
Article

DOI: 10.1007/s10858-005-0165-1

Cite this article as:
Contessa, G.M., Orsale, M., Melino, S. et al. J Biomol NMR (2005) 31: 185. doi:10.1007/s10858-005-0165-1

Abstract

The NMR high-resolution structure of calmodulin complexed with a fragment of the olfactory cyclic-nucleotide gated channel is described. This structure shows features that are unique for this complex, including an active role of the linker connecting the N- and C-lobes of calmodulin upon binding of the peptide. Such linker is not only involved in the formation of an hydrophobic pocket to accommodate a bulky peptide residue, but it also provides a positively charged region complementary to a negative charge of the target. This complex of calmodulin with a target not belonging to the kinase family was used to test the residual dipolar coupling (RDC) approach for the determination of calmodulin binding modes to peptides. Although the complex here characterized belongs to the (1--14) family, high Q values were obtained with all the 1:1 complexes for which crystalline structures are available. Reduction of the RDC data set used for the correlation analysis to structured regions of the complex allowed a clear identification of the binding mode. Excluded regions comprise calcium binding loops and loops connecting the EF-hand motifs.

Keywords

backbone dynamicscalmodulincalmodulin binding modesNMRolfactory CNG channelresidual dipolar couplings

Supplementary material

supp.pdf
Supplementary material

Copyright information

© Kluwer Academic Publishers 2005

Authors and Affiliations

  • Gian Marco Contessa
    • 1
    • 3
  • Maria Orsale
    • 1
  • Sonia Melino
    • 1
  • Vincent Torre
    • 4
  • Maurizio Paci
    • 1
    • 3
  • Alessandro Desideri
    • 2
    • 3
  • Daniel O. Cicero
    • 1
    • 4
  1. 1.Department of Chemical Sciences and TechnologiesUniversity of Rome “Tor Vergata”RomeItaly
  2. 2.Department of BiologyUniversity of Rome “Tor Vergata”RomeItaly
  3. 3.INFMUniversity of Rome “Tor Vergata”RomeItaly
  4. 4.INFM and SISSASettore di BiofisicaTriesteItaly