Structure of human transthyretin complexed with bromophenols: a new mode of binding.

@article{Ghosh2000StructureOH,
  title={Structure of human transthyretin complexed with bromophenols: a new mode of binding.},
  author={Manami Ghosh and Ilonka Meerts and Alison J. Cook and A Bergman and Abraham A. Brouwer and Louise N. Johnson},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2000},
  volume={56 Pt 9},
  pages={
          1085-95
        }
}
The binding of two organohalogen substances, pentabromophenol (PBP) and 2,4,6-tribromophenol (TBP), to human transthyretin (TTR), a thyroid hormone transport protein, has been studied by in vitro competitive binding assays and by X-ray crystallography. Both compounds bind to TTR with high affinity, in competition with the natural ligand thyroxine (T(4)). The crystal structures of the TTR-PBP and TTR-TBP complexes show some unusual binding patterns for the ligands. They bind exclusively in the… CONTINUE READING
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