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J Biol Chem, Vol. 274, Issue 1, 170-174, January 1, 1999
-Lactoglobulin Binds Palmitate within Its Central Cavity
,
From the Bovine
Structural Biochemistry Group, University of
Edinburgh, Swann Building, King's Buildings, Mayfield Road, Edinburgh
EH9 3JR, Scotland and § Tecnologia se los Alimentos,
Veterinary Faculty, University of Zaragoza, Miguel Servet 177, 50013 Zaragoza, Spain
-lactoglobulin (
-Lg) has been
studied extensively in both the isolated and the naturally occurring
states. It is a commercially important whey protein of obvious
nutritional value but, so far, one that has no clearly identified
biological function. In common with many of the other members of the
lipocalin family to which it belongs,
-Lg binds hydrophobic ligands,
and it appears possible that there are at least two distinct binding
sites per monomer for a variety of ligands. By comparison with other
members of the family, there is a probable binding site in the central cavity of the molecule that is formed by the eight antiparallel
-strands that are typical of the lipocalins. We have now
cocrystallized
-Lg with palmitic acid, and the refined structure
(R = 0.204, Rfree = 0.240 for 6,888 reflections to 2.5-Å resolution) reveals that the ligand binds in the
central cavity in a manner similar to the binding of retinol to the
related lipocalin, serum retinol-binding protein. The carboxyl group
binds to both Lys-60 and Lys-69 at the entrance to the cavity. The
hydrophobic tail stretches in an almost fully extended conformation
into the center of the protein. This is the first direct observation of
a ligand binding to
-Lg.
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