Abstract
β-lactoglobulin is a major whey protein of 162 residues and is composed of nine β-strands (A-I strand) and one a -helix. Eight out of the nine strands form an upand-down b -barrel structure. Under physiological conditions, equine βlactoglobulin (ELG) is monomer, whereas bovine β-lactoglobulin (BLG) exists as a dimer in which I strand forms an intermolecular β-sheet. In this study, we report the 2.0 resolution crystal structure of Gyuba which was constructed from the amino acid sequences of secondary-structured regions of BLG and those of loop regions of ELG. This structure revealed that Gyuba formed dimer in which I strand forms an intermolecular β-sheet. This dimerization is similar to BLG.
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