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

@article{Ikura1992SolutionSO,
  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},
  journal={Science},
  year={1992},
  volume={256 5057},
  pages={
          632-8
        }
}
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… 
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TLDR
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.
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TLDR
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Peptide binding by a fragment of calmodulin composed of EF-hands 2 and 3.
TLDR
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.
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TLDR
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.
TLDR
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
TLDR
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.
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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.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
The results of these studies indicate that the catalytic and calmodulin-binding domains of MLCK represent distinct and separable regions of the protein.
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TLDR
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.
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