reviewJournal of Dairy ScienceApr 1, 2004BRONZE OA

Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function

University of Edinburgh · Hannah Research Foundation

PubMed
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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

722
total citations
FWCI
17.28
Percentile
100%
References
64
Citations per year

Authors

3

Topics & keywords

Keywords
  • Chemistry
  • Dimer
  • Protein structure
  • Binding site
  • Ligand (biochemistry)
  • Crystallography
  • Stereochemistry
  • Biochemistry
UN Sustainable Development Goals
  • Life in Land
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