Calcium-induced conformational transition revealed by the solution structure of apo calmodulin

@article{Zhang1995CalciuminducedCT,
  title={Calcium-induced conformational transition revealed by the solution structure of apo calmodulin},
  author={Mingjie Zhang and Toshiyuki Tanaka and Mitsuhiko Ikura},
  journal={Nature Structural Biology},
  year={1995},
  volume={2},
  pages={758-767}
}
The solution structure of Ca2+-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca2+-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36°–44°. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H… Expand
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TLDR
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Structure of a trapped intermediate of calmodulin: calcium regulation of EF-hand proteins from a new perspective.
  • Z. Grabarek
  • Chemistry, Medicine
  • Journal of molecular biology
  • 2005
TLDR
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Ca2+ binding sites in calmodulin and troponin C alter interhelical angle movements
TLDR
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Ligand binding and thermodynamic stability of a multidomain protein, calmodulin
TLDR
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Solvation energetics and conformational change in EF‐hand proteins
TLDR
It is shown the importance of a precise balance of solvation energetics to conformational change, using mutational analysis of partially buried polar groups in the N‐terminal domain of calmodulin (N‐cam). Expand
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. Expand
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