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

  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},
  volume={275 42},
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


Publications citing this paper.
Showing 1-10 of 21 extracted citations

Ribonucleotide reductase as a target to control apicomplexan diseases.

Current issues in molecular biology • 2012
View 4 Excerpts
Highly Influenced

dNTP pool levels modulate mutator phenotypes of error-prone DNA polymerase ε variants.

Proceedings of the National Academy of Sciences of the United States of America • 2015

Similar Papers

Loading similar papers…