Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function
University of Edinburgh · Hannah Research Foundation
Abstract
Beta-Lactoglobulin (beta-LG) is the major whey protein of ruminant species and is also present in the milks of many, but not all, other species. Its amino-acid sequence and 3-dimensional structure show that it is a lipocalin, a widely diverse family, most of which bind small hydrophobic ligands and thus may act as specific transporters, as does serum retinol binding protein. Bovine beta-LG binds a wide range of ligands, but this may not be the reason for its presence in milk. In reviewing the structure and physicochemical properties of the protein, we present the structures of the ligands cholesterol (at a resolution of 2.0A, R = 0.221; Rfree = 0.295) and vitamin D2 (at a resolution of 2.4A, R = 0.212; Rfree =…
Citation impact
- FWCI
- 17.28
- Percentile
- 100%
- References
- 64
Authors
3Topics & keywords
- Chemistry
- Dimer
- Protein structure
- Binding site
- Ligand (biochemistry)
- Crystallography
- Stereochemistry
- Biochemistry
- Life in Land