Grouping together highly diverged PD-(D/E)XK nucleases and identification of novel superfamily members using structure-guided alignment of sequence profiles.

@article{Bujnicki2001GroupingTH,
  title={Grouping together highly diverged PD-(D/E)XK nucleases and identification of novel superfamily members using structure-guided alignment of sequence profiles.},
  author={Janusz M. Bujnicki and Leszek Rychlewski},
  journal={Journal of molecular microbiology and biotechnology},
  year={2001},
  volume={3 1},
  pages={69-72}
}
The PD-(D/E)XK nuclease domains, initially identified in type II restriction enzymes, serve as models for studying aspects of protein-DNA interactions, mechanisms of phosphodiester hydrolysis, and provide indispensable tools for techniques in genetic engineering and molecular medicine. However, the low degree of amino acid conservation hampers the possibility of identification of PD-(D/E)XK superfamily members based solely on sequence comparisons. In several proteins implicated in DNA… CONTINUE READING

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Sequence-structure-function relationships in the evolution of nucleic acid enzymes

  • J. M. Bujnicki
  • Ph.D. thesis [in Polish]. Warsaw University.
  • 2000
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