1gx9
From Proteopedia
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BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH RETINOIC ACID, TRIGONAL LATTICE Z
Overview
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 Structure
1GX9 is a [Single protein] structure of sequence from [Bos taurus] with REA as [ligand]. Structure known Active Site: REA. Full crystallographic information is available from [OCA].
Reference
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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