Structural highlights
Function
[LACB_SHEEP] Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
Publication Abstract from PubMed
The crystal structure of the triclinic form of the milk protein beta-lactoglobulin from sheep (Ovis aries) at 1.1 A resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.
Ovine beta-lactoglobulin at atomic resolution.,Kontopidis G, Nordle Gilliver A, Sawyer L Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1498-503. doi:, 10.1107/S2053230X14020950. Epub 2014 Oct 31. PMID:25372816[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kontopidis G, Nordle Gilliver A, Sawyer L. Ovine beta-lactoglobulin at atomic resolution. Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1498-503. doi:, 10.1107/S2053230X14020950. Epub 2014 Oct 31. PMID:25372816 doi:http://dx.doi.org/10.1107/S2053230X14020950
