Abstract
Calmodulin (CaM) acts as an intracellular calcium sensor that translates the Ca2+ signal into a variety of cellular processes. Ca(2+)-CaM recognition of a short polypeptide segment in target proteins induces conformational changes in both CaM and the target, enabling the target protein to become functionally active. The solution and crystal structures of Ca(2+)-CaM bound to peptides derived from three CaM-dependent enzymes reveal structural features that are common in target recognition by Ca(2+)-CaM. Phosphorylation of the target proteins at sites in or near the CaM-binding region modulates binding of CaM, thereby providing an additional mechanism of functional regulation. The structural aspects of target recognition by Ca(2+)-CaM are discussed using mainly the three-dimensional structural information obtained with nuclear magnetic resonance spectroscopy and X-ray diffraction methods.
Keywords
CalmodulinBiophysicsChemistryMolecular recognitionIntracellularCalcium-binding proteinStructural biologyPlasma protein bindingCell biologyBiochemistryCalciumCrystallographyEnzymeBiologyMolecule
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Publication Info
- Year
- 1995
- Type
- review
- Volume
- 24
- Issue
- 1
- Pages
- 85-116
- Citations
- 754
- Access
- Closed
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Cite This
Anna Crivici,
Mitsuhiko Ikura
(1995).
Molecular and Structural Basis of Target Recognition by Calmodulin.
Annual Review of Biophysics and Biomolecular Structure
, 24
(1)
, 85-116.
https://doi.org/10.1146/annurev.bb.24.060195.000505
Identifiers
- DOI
- 10.1146/annurev.bb.24.060195.000505