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.Abstract
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
Add to ORKG