Ligand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor protein.

@article{Taraban2008LigandinducedCC,
  title={Ligand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor protein.},
  author={Marc Taraban and Hongli Zhan and Andrew E. Whitten and David B Langley and Kathleen Shive Matthews and Liskin Swint-Kruse and Jill Trewhella},
  journal={Journal of molecular biology},
  year={2008},
  volume={376 2},
  pages={466-81}
}
We present here the results of a series of small-angle X-ray scattering studies aimed at understanding the role of conformational changes and structural flexibility in DNA binding and allosteric signaling in a bacterial transcription regulator, lactose repressor protein (LacI). Experiments were designed to detect possible conformational changes that occur when LacI binds either DNA or the inducer IPTG, or both. Our studies included the native LacI dimer of homodimers and a dimeric variant (R3… CONTINUE READING

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