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Solution structure of a mammalian PCB-binding protein in complex with a PCB

Nature Structural Biology volume 2, pages 983–989 (1995)Cite this article

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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Author information

Author notes

  1. Henry J. Barnes

    Present address: Immune Complex Corporation, 11099 N.Torrey Pines Road Suite 240, La Jolla, California, 92037, USA

Authors and Affiliations

  1. Center for Structural Biochemistry, Karolinska Institutet NOVUM, S-14157, Huddinge, Sweden

    Torleif Härd

  2. Department of Medical Nutrition, Karolinska Institutet NOVUM, S-14157, Huddinge, Sweden

    Henry J. Barnes, Jan-Åke Gustafsson & Johan Lund

  3. Department of Environmental Chemistry, Wallenberg Laboratory, Stockholm University, S-106 91, Stockholm, Sweden

    Christina Larsson

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  3. Christina Larsson
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  4. Jan-Åke Gustafsson
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  5. Johan Lund
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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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