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Contents |
Alpha Lactalbumin
α-lactalbumin is a small globular protein which is stabilized by four disulfide bonds with two structural domains. One domain is rich in α-helices, the other is rich in β-sheets and has a calcium binding site. [1] α-lactalbumin is a major protein in all kinds of milk studied so far. [2] α- lactalbumin contributes to cell lytic activity, cell growth inhibition, and apoptosis but most importantly, it interacts with UDP-galactosyltransferase [2] to form lactose synthetase via the following reaction:
UDP-galactose + glucose -+ lactose + UDP [3]
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| 1a4v, resolution 1.80Å () | |||||||||
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| Ligands: | |||||||||
| Activity: | Lactose synthase, with EC number 2.4.1.22 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Structure
: with alpha helices shown in pink rockets, and beta sheets shown in yellow planks.
: with nonpolar side chains in gray, polar side chains in purple, and associated water molecules in red.
: calcium ligands with amino acid contacts. water in pink, oxygen in red.
Function
Recent Studies
References
- ↑ Hendrix TM, Griko Y, Privalov P. 1996. Energetics of structural domains in α-lactalbumin. Protein Science. 5923-5931.
- ↑ 2.0 2.1 Vilotte JL. Alpha-lactalbumin: Gene Structure and Expression. <http://mammary.nih.gov/Reviews/gene_expression/Vilotte001/index.html>.
- ↑ Fitzgerald DK, Brodbeck URS, Kiyosawa I, Mawal R, Colvin B, Ebner KE. 1970. α-lactalbumin and the Lactose Synthetase Reaction. The Journal of Biological Chemistry. 245(8): 2103-2108.
