Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics.

@article{Laine2008AllostericSI,
  title={Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics.},
  author={Olli Laine and E. D. Streaker and Maryam Nabavi and C. Fenselau and D. Beckett},
  journal={Journal of molecular biology},
  year={2008},
  volume={381 1},
  pages={
          89-101
        }
}
  • Olli Laine, E. D. Streaker, +2 authors D. Beckett
  • Published 2008
  • Chemistry, Medicine
  • Journal of molecular biology
  • The biotin repressor is an allosterically regulated, site-specific DNA-binding protein. Binding of the small ligand bio-5'-AMP activates repressor dimerization, which is a prerequisite to DNA binding. Multiple disorder-to-order transitions, some of which are known to be important for the functional allosteric response, occur in the vicinity of the ligand-binding site concomitant with effector binding to the repressor monomer. In this work, the extent to which these local changes are coupled to… CONTINUE READING
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