Comparative Study
doi: 10.1126/science.1763327.
Identification and characterization of zinc binding sites in protein kinase C
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- PMID: 1763327
- DOI: 10.1126/science.1763327
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Comparative Study
Identification and characterization of zinc binding sites in protein kinase C
Science.
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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 beta I overexpressed in insect cells, direct evidence has been obtained that PKC beta I tightly binds four zinc ions (Zn2+) per molecule. Extended x-ray absorption fine structure (EXAFS) data are best fit by an average Zn2+ coordination of one nitrogen and three sulfur atoms. Of the plausible Zn2+ coordination models, only those featuring nonbridged Zn2+ sites accommodate the EXAFS data and all of the conserved potential ligands.
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