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Identification and Characterization of Zinc Binding Sites in Protein Kinase C
Abstract
Metal ion coordination in the regulatory domain of protein kinase C (PKC) is suggested by the conservation of six cysteines and two histidines in two homologous regions found therein. By monitoring x-ray fluorescence from a purified sample of rat PKC βI overexpressed in insect cells, direct evidence has been obtained that PKC βI tightly binds four zinc ions (Zn 2+ ) per molecule. Extended x-ray absorption fine structure (EXAFS) data are best fit by an average Zn 2+ coordination of one nitrogen and three sulfur atoms. Of the plausible Zn 2+ coordination models, only those featuring nonbridged Zn 2+ sites accommodate the EXAFS data and all of the conserved potential ligands.
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Citations
Cited by
The extended protein kinase C superfamily
MELLOR, H., & PARKER, P. J. (1998) · Biochemical Journal · doi:10.1042/bj3320281 · Cited by 1,538
Zinc coordination sphere in biochemical zinc sites
Auld, D. S. (2001) · Biometals · doi:10.1023/a:1012976615056 · Cited by 721
Selbie, L. A., Schmitz-Peiffer, C., Sheng, Y., & Biden, T. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80525-0 · Cited by 349
Maywald, M., Wessels, I., & Rink, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102222 · Cited by 309
Metal Complexes as Enzyme Inhibitors
Louie, A. Y., & Meade, T. J. (1999) · Chemical Reviews · doi:10.1021/cr9804285 · Cited by 301
Metadata
- Authors
- Hubbard, S. R., Bishop, W. R., Kirschmeier, P., George, S. J., Cramer, S. P., & Hendrickson, W. A.
- Venue
- Science
- Published
- 1991-12-20
- Volume
- 254
- Issue
- 5039
- Pages
- 1776-1779
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2048116173
- Cited by
- 193
- References
- 0
- FWCI
- 22.57
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hubbard, S. R., Bishop, W. R., Kirschmeier, P., George, S. J., Cramer, S. P., & Hendrickson, W. A. (1991). Identification and Characterization of Zinc Binding Sites in Protein Kinase C. Science. https://doi.org/10.1126/science.1763327
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