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FEBS Lett. 2014 Nov 3;588(21):3816-22. doi: 10.1016/j.febslet.2014.09.010. Epub 2014 Sep 18.

Ultra-high resolution crystal structure of recombinant caprine β-lactoglobulin.

Author information

1
Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.
2
Institute of Fundamental Sciences and The Riddet Institute, Massey University, Palmerston North, New Zealand.
3
Food and Bio-based Products, AgResearch Limited, Ruakura Research Centre, Hamilton, New Zealand.
4
Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch, New Zealand; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia. Electronic address: renwick.dobson@canterbury.ac.nz.

Abstract

β-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 (K(D)<5 μM); 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.

KEYWORDS:

Analytical ultracentrifugation; Caprine; Goat; Milk whey; Small-angle X-ray scattering; Ultra-high resolution structure

PMID:
25241165
DOI:
10.1016/j.febslet.2014.09.010
[Indexed for MEDLINE]
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