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Molecular and Structural Basis of Target Recognition by Calmodulin
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.
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Cited by
Ultrasensitive fluorescent proteins for imaging neuronal activity
Chen, T.-W., Wardill, T. J., Sun, Y., Pulver, S. R., Renninger, S. L., Baohan, A., Schreiter, E. R., Kerr, R. A., Orger, M. B., Jayaraman, V., et al. (2013) · Nature · doi:10.1038/nature12354 · Cited by 6,474
Fluorescent indicators for Ca2+based on green fluorescent proteins and calmodulin
Miyawaki, A., Llopis, J., Heim, R., McCaffery, J. M., Adams, J. A., Ikura, M., & Tsien, R. Y. (1997) · Nature · doi:10.1038/42264 · Cited by 3,248
Self-citationThe Conformational Plasticity of Protein Kinases
Huse, M., & Kuriyan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00741-9 · Cited by 1,752
Coupling of folding and binding for unstructured proteins
Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327
Generation, Control, and Processing of Cellular Calcium Signals
Carafoli, E., Santella, L., Branca, D., & Brini, M. (2001) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/20014091074183 · Cited by 531
Metadata
- Authors
- Crivici, A., & Ikura, M.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 1995-06
- Volume
- 24
- Issue
- 1
- Pages
- 85-116
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2172712627
- Cited by
- 757
- References
- 0
- FWCI
- 13.03
- Type
- journal article
- Language
- en
- Open access
- closed
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- Crivici, A., & Ikura, M. (1995). Molecular and Structural Basis of Target Recognition by Calmodulin. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.bb.24.060195.000505
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