The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
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. © 1986 Nature Publishing Group.
Publication Source (Journal or Book title)
Papiz, M., Sawyer, L., Eliopoulos, E., North, A., Findlay, J., Sivaprasadarao, R., Jones, T., Newcomer, M., & Kraulis, P. (1986). The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature, 324 (6095), 383-385. https://doi.org/10.1038/324383a0