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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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

Since its first isolation, bovine beta-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 A. It has an unusual protein fold, composed of two slabs of antiparallel beta-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.[1]

References

  1. The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein. Papiz, M.Z., Sawyer, L., Eliopoulos, E.E., North, A.C., Findlay, J.B., Sivaprasadarao, R., Jones, T.A., Newcomer, M.E., Kraulis, P.J. Nature (1986) [Pubmed]
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