CaBP Data Library General Information

Information in the EF-Hand Calcium-Binding Proteins Database from Reference 205

Protein
 Species
 Information
 Comment
 Submitted By
 Validated By
calmodulin
isoform 1
the main isoform, and the only isoform found in most species
 Drosophila melanogaster
(fruit fly)
 structure by NMR (pdb entry 2BBN) of full length protein
  • bound to 4 ions of Ca
  • bound to 1 equivalent of the following portion of skeletal muscle myosin light chain kinase: peptide derived from the calmodulin binding domain of the skeletal muscle myosin light chain kinase
Melanie R. Nelson
The Scripps Research Institute, Department of Molecular Biology
mnelson@scripps.edu
 Melanie R. Nelson
mnelson@scripps.edu
calmodulin
isoform 1
the main isoform, and the only isoform found in most species
 no species information The conformational change between four calcium ions bound and four calcium ions and target peptide bound states involves:
  • Target peptide binding to calcium-loaded calmodulin effects mainly the quarternary structure: the structure of the two domains is not changed.
    In the absence of peptide, the two domains do not interact to a large extent, and the linekr between the two domains is flexible. Peptide binding causes calmodulin to compact, as the two domains wrap around the target peptide, with CaM-C interacting with the N-terminal portion of one face of the peptide and CaM-N interacting with the C-terminal portion of the other face.
    The flexible nature of the tether between the two domains allows calmodulin to bind to peptides of varying length.
 This si the reference for the NMR strucutre of calmodulin bound to a peptide from myosin light chain kinase. A similar crystal structure was subsequently solved: [ref_num 299]. The role of the flexible linker in allowing calmodulin to bind peptides of different lengths is discussed in the paper reporting the crystal strucutre of calmodulin complexed with a peptide derived from calcium/calmodulin-dependent protein kinase II: [ref_num 298].
 Melanie R. Nelson
The Scripps Research Institute, Department of Molecular Biology
mnelson@scripps.edu
 Melanie R. Nelson
mnelson@scripps.edu