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The structure of -lactoglobulin and its similarity to plasma retinol-binding protein M. Z. Papiz*†, L. Sawyer*‡§, E. E. Eliopoulos , A. C. T. North , J. B. C. Findlay¶, R. Sivaprasadarao¶, T. A. Jones£, M. E. Newcomer£ & P. J. Kraulis£
*Department of Applied Chemical Sciences, Napier College, Edinburgh EH10 5DT, UK
‡Department of Biochemistry, University of Edinburgh, Edinburgh EH8 9XD, UK
Astbury Department of Biophysics, University of Leeds, Leeds LS2 9JT, UK
¶Department of Biochemistry, University of Leeds, Leeds LS2 9JT, UK
£Department of Molecular Biology, Box 590, BMC University of Uppsala, Uppsala, Sweden
†Present address: SERC Daresbury Laboratory, Warrington WA4 4AD, UK.
§To whom correspondence should be addressed.
Since its first isolation1, bovine -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 -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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