Title

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

Document Type

Article

Publication Date

12-1-1986

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. © 1986 Nature Publishing Group.

Publication Source (Journal or Book title)

Nature

First Page

383

Last Page

385

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