Structural highlights
Function
[LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Allergies are caused by the immune reaction to commonly harmless proteins, allergens. This reaction is typified by immunoglobulin E (IgE) antibodies. We report the crystal structure of an IgE Fab fragment in complex with beta-lactoglobulin (BLG), one of the major allergens of bovine milk. The solved structure shows how two IgE/Fab molecules bind the dimeric BLG. The epitope of BLG consists of six different short fragments of the polypeptide chain, which are located especially in the beta strands, covering a flat area on the allergen surface. All six CDR (complementary-determining region) loops of the IgE Fab participate in the binding of BLG. The light chain CDR loops are responsible for the binding of the flat beta sheet region of BLG. The IgE epitope is different from common IgG epitopes that are normally located in the exposed loop regions of antigens and observed also in the two recently determined allergen-IgG complexes.
Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen.,Niemi M, Jylha S, Laukkanen ML, Soderlund H, Makinen-Kiljunen S, Kallio JM, Hakulinen N, Haahtela T, Takkinen K, Rouvinen J Structure. 2007 Nov;15(11):1413-21. PMID:17997967[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Niemi M, Jylha S, Laukkanen ML, Soderlund H, Makinen-Kiljunen S, Kallio JM, Hakulinen N, Haahtela T, Takkinen K, Rouvinen J. Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen. Structure. 2007 Nov;15(11):1413-21. PMID:17997967 doi:10.1016/j.str.2007.09.012
