Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives.

@article{Ni2000InsightsIN,
  title={Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives.},
  author={Qing Ni and Jennifer R Shaffer and Joseph A. Adams},
  journal={Protein science : a publication of the Protein Society},
  year={2000},
  volume={9 9},
  pages={1818-27}
}
The binding of the methylanthraniloyl derivatives of ATP (mant-ATP), ADP (mant-ADP), 2'deoxyATP (mant-2'deoxyATP), and 3'deoxyATP (mant-3'deoxyATP) to the catalytic subunit of protein kinase A was studied to gain insights into the mechanism of nucleotide binding. The binding of the mant nucleotides leads to a large increase in fluorescence energy transfer at 440 nm, allowing direct measurements of nucleotide affinity. The dissociation constant of mant-ADP is identical to that for ADP, while… CONTINUE READING

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