Structural highlights
Function
[LACB_CAPHI] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
Publication Abstract from PubMed
beta-Lactoglobulin (betalg) is the most abundant whey protein in the milks of ruminant animals. While bovine betalg 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 betalg complemented by analytical ultracentrifugation and small-angle X-ray scattering data. In both solution and crystalline states caprine betalg is dimeric (KD<5muM); 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.
Ultra-high resolution crystal structure of recombinant caprine beta-lactoglobulin.,Crowther JM, Lasse M, Suzuki H, Kessans SA, Loo TS, Norris GE, Hodgkinson AJ, Jameson GB, Dobson RC FEBS Lett. 2014 Sep 18. pii: S0014-5793(14)00685-1. doi:, 10.1016/j.febslet.2014.09.010. PMID:25241165[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Crowther JM, Lasse M, Suzuki H, Kessans SA, Loo TS, Norris GE, Hodgkinson AJ, Jameson GB, Dobson RC. Ultra-high resolution crystal structure of recombinant caprine beta-lactoglobulin. FEBS Lett. 2014 Sep 18. pii: S0014-5793(14)00685-1. doi:, 10.1016/j.febslet.2014.09.010. PMID:25241165 doi:http://dx.doi.org/10.1016/j.febslet.2014.09.010
