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Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex
Abstract
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 to a resolution of 2.4 angstroms (Å). The structure is compact and has the shape of an ellipsoid (axial ratio ∼2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (<4 Å) are formed between CaM and the peptide, with van der Waals contacts comprising ∼80% of this total.
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Citations
Cited by
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Dynamic personalities of proteins
Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
Metadata
- Authors
- Meador, W. E., Means, A. R., & Quiocho, F. A.
- Venue
- Science
- Published
- 1992-08-28
- Volume
- 257
- Issue
- 5074
- Pages
- 1251-1255
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1987159249
- Cited by
- 1,033
- References
- 0
- FWCI
- 25.32
- Type
- journal article
- Language
- en
- Open access
- closed
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- Meador, W. E., Means, A. R., & Quiocho, F. A. (1992). Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex. Science. https://doi.org/10.1126/science.1519061
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
