Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase.

@article{Reichard2000CrosstalkBT,
  title={Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase.},
  author={Peter A Reichard and Rolf Eliasson and Rolf Ingemarson and Lars Thelander},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 42},
  pages={33021-6}
}
We compared the allosteric regulation and effector binding properties of wild type R1 protein and R1 protein with a mutation in the "activity site" (D57N) of mouse ribonucleotide reductase. Wild type R1 had two effector-binding sites per polypeptide chain: one site (activity site) for dATP and ATP, with dATP-inhibiting and ATP-stimulating catalytic activity; and a second site (specificity site) for dATP, ATP, dTTP, and dGTP, directing substrate specificity. Binding of dATP to the specificity… CONTINUE READING

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