Abstract
Metabolites of polychlorinated biphenyls (PCBs) bind with high affinity to uteroglobin, a small homodimeric protein that also binds progesterone. We present the solution structure of the reduced form of rat uteroglobin in complex with a PCB methylsulphone, (MeSO2)2-TCB. The structure reveals the molecular basis for the accumulation of (MeSO2)2-TCB by uteroglobin. The structure also shows how ligand binding and release might be controlled by reduction/oxidation of two intermolecular disulphide bonds. Breakage of these bonds induces a local unfolding of the N- and C-termini and a separation of helices creating a channel into the binding site. These effects make the ligand binding cavity readily accessible to entry of the ligand.
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Härd, T., Barnes, H., Larsson, C. et al. Solution structure of a mammalian PCB-binding protein in complex with a PCB. Nat Struct Mol Biol 2, 983–989 (1995). https://doi.org/10.1038/nsb1195-983
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DOI: https://doi.org/10.1038/nsb1195-983
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