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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chemical Phenomena
  • Crystallography, X-Ray
  • Goats*
  • Lactoglobulins / chemistry*
  • Lactoglobulins / genetics
  • Lactoglobulins / isolation & purification
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Quaternary
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification


  • Lactoglobulins
  • Recombinant Proteins