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
Using heteronuclear NMR spectroscopy, we studied the solution structure and dynamics of bovine beta-lactoglobulin A at pH 2.0 and 45 degrees C, where the protein exists as a monomeric native state. The monomeric NMR structure, comprising an eight-stranded continuous antiparallel beta-barrel and one major alpha-helix, is similar to the X-ray dimeric structure obtained at pH 6.2, including betaI-strand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. [1H]-15N NOE revealed that betaF, betaG, and betaH strands buried under the major alpha-helix are rigid on a pico- to nanosecond time scale and also emphasized rapid fluctuations of loops and the N- and C-terminal regions.
Solution structure and dynamics of bovine beta-lactoglobulin A.,Kuwata K, Hoshino M, Forge V, Era S, Batt CA, Goto Y Protein Sci. 1999 Nov;8(11):2541-5. PMID:10595563[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kuwata K, Hoshino M, Forge V, Era S, Batt CA, Goto Y. Solution structure and dynamics of bovine beta-lactoglobulin A. Protein Sci. 1999 Nov;8(11):2541-5. PMID:10595563
