1gx8
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BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH RETINOL, TRIGONAL LATTICE Z
OverviewOverview
Ever since the fortuitous observation that beta-lactoglobulin (beta-Lg), the major whey protein in the milk of ruminants, bound retinol, the, details of the binding have been controversial. beta-Lg is a lipocalin, like plasma retinol-binding protein, so that ligand association was, expected to make use of the central cavity in the protein. However, an, early crystallographic analysis and some of the more recent solution, studies indicated binding elsewhere. We have now determined the crystal, structures of the complexes of the trigonal form of beta-Lg at pH 7.5 with, bound retinol (R=21.4% for 7329 reflections between 20 and 2.4 A, resolution, R(free)=30.6%) and with bound retinoic acid (R=22.7% for 7813, reflections between 20 and 2.34 A resolution, R(free)=29.8%). Both ligands, are ... [(full description)]
About this StructureAbout this Structure
1GX8 is a [Single protein] structure of sequence from [Bos taurus] with RTL as [ligand]. Structure known Active Site: RTL. Full crystallographic information is available from [OCA].
ReferenceReference
The ligand-binding site of bovine beta-lactoglobulin: evidence for a function?, Kontopidis G, Holt C, Sawyer L, J Mol Biol. 2002 May 10;318(4):1043-55. PMID:12054801
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