Structure of the DNA repair helicase hel308 reveals DNA binding and autoinhibitory domains.

@article{Richards2008StructureOT,
  title={Structure of the DNA repair helicase hel308 reveals DNA binding and autoinhibitory domains.},
  author={Jodi D Richards and K A Johnson and Huanting Liu and Anne-Marie McRobbie and Stephen A. McMahon and Muse Oke and Lester G. Carter and James H. Naismith and Malcolm F White},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 8},
  pages={5118-26}
}
Hel308 is a superfamily 2 helicase conserved in eukaryotes and archaea. It is thought to function in the early stages of recombination following replication fork arrest and has a specificity for removal of the lagging strand in model replication forks. A homologous helicase constitutes the N-terminal domain of human DNA polymerase Q. The Drosophila homologue mus301 is implicated in double strand break repair and meiotic recombination. We have solved the high resolution crystal structure of… CONTINUE READING
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