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The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein

Nature volume 324, pages 383–385 (1986)Cite this article

Abstract

Since its first isolation1, bovine β-lactoglobulin (BLG) has been an enigma: although it is abundant in the whey fraction of milk, its function is still not clear. The results of the many physicochemical studies on the protein need a structural interpretation. We report here the structure of the orthorhombic crystal form of cow BLG at pH 7.6, at a resolution of 2.8 Å. It has an unusual protein fold, composed of two slabs of antiparallel β-sheet, which shows a remarkable similarity to plasma retinol-binding protein. A possible binding site for retinol in BLG has been identified by model-building. This suggests a role for BLG in vitamin A transport and we have discovered specific receptors for the BLG–retinol complex in the intestine of neonate calves.

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Author notes

  1. M. Z. Papiz

    Present address: SERC Daresbury Laboratory, Warrington, WA4 4AD, UK

Authors and Affiliations

  1. Department of Applied Chemical Sciences, Napier College, Edinburgh, EH10 5DT, UK

    M. Z. Papiz & L. Sawyer

  2. Department of Biochemistry, University of Edinburgh, Edinburgh, EH8 9XD, UK

    L. Sawyer

  3. Astbury Department of Biophysics, University of Leeds, Leeds, LS2 9JT, UK

    E. E. Eliopoulos & A. C. T. North

  4. Department of Biochemistry, University of Leeds, Leeds, LS2 9JT, UK

    J. B. C. Findlay & R. Sivaprasadarao

  5. Department of Molecular Biology, BMC University of Uppsala, Box 590, Uppsala, Sweden

    T. A. Jones, M. E. Newcomer & P. J. Kraulis

Authors
  1. M. Z. Papiz
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  2. L. Sawyer
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  3. E. E. Eliopoulos
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  4. A. C. T. North
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  5. J. B. C. Findlay
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  7. T. A. Jones
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  9. P. J. Kraulis
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Papiz, M., Sawyer, L., Eliopoulos, E. et al. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324, 383–385 (1986). https://doi.org/10.1038/324383a0

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