4tlj

Ultra-high resolution crystal structure of caprine Beta-lactoglobulin

spinqualitylabelsall models 4tlj, resolution 1.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tlj is a 2 chain structure with sequence from Capra hircus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.17Å Ligands: BU1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactoglobulin 3D structures

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