Ultra-high resolution crystal structure of recombinant caprine β-lactoglobulin
- Crowther, Jennifer M.
- Lassé, Moritz
- Suzuki, Hironori
- Kessans, Sarah A.
- Loo, Trevor S.
- Norris, Gillian E.
- Hodgkinson, Alison J.
- Jameson, Geoffrey B.
- Dobson, Renwick C.J.
Publication date
November 2014
DOI Publisher
Federation of European Biochemical Societies. Published by Elsevier B.V. ISSN
0014-5793 Citation count (estimate)
5Abstract
Abstractβ-Lactoglobulin (βlg) is the most abundant whey protein in the milks of ruminant animals. While bovine βlg has been subjected to a vast array of studies, little is known about the caprine ortholog. We present an ultra-high resolution crystal structure of caprine βlg complemented by analytical ultracentrifugation and small-angle X-ray scattering data. In both solution and crystalline states caprine βlg is dimeric (KD<5μM); however, our data suggest a flexible quaternary arrangement of subunits within the dimer. These structural findings will provide insight into relationships among structural, processing, nutritional and immunological characteristics that distinguish cow’s and goat’s milk
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