Solution structure of a calmodulin-target peptide complex by multidimensional NMR.

  title={Solution structure of a calmodulin-target peptide complex by multidimensional NMR.},
  author={Mitsuhiko Ikura and G. Marius Clore and Angela M. Gronenborn and Guang Zhu and Claude B. Klee and Adriaan Bax},
  volume={256 5057},
The three-dimensional solution structure of the complex between calcium-bound calmodulin (Ca(2+)-CaM) and a 26-residue synthetic peptide comprising the CaM binding domain (residues 577 to 602) of skeletal muscle myosin light chain kinase, has been determined using multidimensional heteronuclear filtered and separated nuclear magnetic resonance spectroscopy. The two domains of CaM (residues 6 to 73 and 83 to 146) remain essentially unchanged upon complexation. The long central helix (residues 65… 
Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.
The crystal structure of calcium-bound calmodulin (Ca(2+)-CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined
Bending of the calmodulin central helix: A theoretical study
The results of the molecular dynamics simulations reproduce the experimentally determined location of the bend in a simulation of only the CaM central helix, indicating that the bending point is an intrinsic property of the α‐helix, for which the remainder of the protein is not important.
The calmodulin-binding domain of caldesmon binds to calmodulin in an alpha-helical conformation.
Two dimensional NMR studies performed in aqueous TFE mixture showed that the CaD peptide has the capacity to adopt an amphiphilic alpha-helical conformation and chemical shifts suggest that both domains and the central helix of CaM are involved in the binding of the peptide.
Peptide binding by a fragment of calmodulin composed of EF-hands 2 and 3.
It is demonstrated that Ca2+-ligated CaM2/3 can also bind to a peptide representing the CaM-recognition sequence of skeletal muscle myosin light chain kinase (M13) with an equimolar stoichiometry and a dissociation constant of 0.40 +/- 0.05 microM.
Protein engineering and NMR studies of calmodulin
The features of CaM, which allow it to be rather promiscous, and bind effectively to all these distinct domains are discussed, and the role of the methionine-rich hydrophobic surfaces of the protein in providing a malleable and sticky surface for binding many hydrophilic peptides is described.
A molecular dynamics study of Ca(2+)-calmodulin: evidence of interdomain coupling and structural collapse on the nanosecond timescale.
A 20-ns molecular dynamics simulation of Ca(2+)-calmodulin (CaM) in explicit solvent is described, which shows a compact shape similar in dimension to complexes of CaM and target peptides but with a substantially different orientation between the N- and C-terminal domains.
Structure and dynamics of calmodulin in solution.
The complex structure of calmodulin bound to a calcineurin peptide
The experiments suggest that the dimeric CaM/CaMBD complex exists in solution, which is unambiguously validated using a carefully‐designed CaM‐sepharose pull‐down experiment.


Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin.
These studies provide the first direct confirmation of the amphiphilic helix model for the structure of peptides bound to calcium-saturated calmodulin, and are generally indicative of helical secondary structure.
Crystal structure of calmodulin.
Structural characterization of the interactions between calmodulin and skeletal muscle myosin light chain kinase: effect of peptide (576-594)G binding on the Ca2+-binding domains.
It is found that the peptide stabilizes the Ca2+-bound state of calmodulin, implying that the apparent inconsistency of the crystal structure with recently reported low-angle X-ray scattering profiles of CaM may lie within the putative central helix bridging the globular domains.
Changes in the structure of calmodulin induced by a peptide based on the calmodulin-binding domain of myosin light chain kinase.
Small-angle X-ray and neutron scattering data support the hypothesis that the interconnecting helix region observed in the crystal structure for calmodulin is quite flexible in solution, allowing the two lobes of cal modulin to form close contacts on binding the peptide.
Isotope-filtered 2D NMR of a protein-peptide complex: study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin
Improved isotope-filtered two-dimensional NMR techiques were developed for suppressing NMR calmodulin signals and demonstrated that residues Arg-3 through Ser-21 of the bound peptide form an a-helix.
Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain.
Results indicate that residues located between position 23 and 41 of the native enzyme contribute significantly to the binding of CaM although the involvement of residues from additional sites is not excluded.
Small-angle X-ray scattering study of calmodulin bound to two peptides corresponding to parts of the calmodulin-binding domain of the plasma membrane Ca2+ pump.
The interaction between calmodulin (CaM) and two synthetic peptides, C20W and C24W, corresponding to parts of the calmodulin-binding domain of the Ca2+ pump of human erythrocytes, has been studied by
Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution.
The crystal structure of calmodulin from Drosophila melanogaster as expressed in a bacterial system has been determined and refined at 2.2-A resolution and reveals a number of significant differences between the two structures.
Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase.
  • D. Blumenthal, K. Takio, E. Krebs
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1985
The results of these studies indicate that the catalytic and calmodulin-binding domains of MLCK represent distinct and separable regions of the protein.
Interaction of calmodulin with the calmodulin binding domain of the plasma membrane Ca2+ pump.
Circular dichroism experiments have shown that it interacted with the calmodulin binding domain, supporting the suggestion that the latter, or a portion of it, may act as a natural inhibitor of the pump.