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PDBsum entry 6ghh
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Transport protein
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PDB id
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6ghh
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References listed in PDB file
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Key reference
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Title
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Thermodynamic, Crystallographic and computational studies of non-Mammalian fatty acid binding to bovine β-Lactoglobulin.
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Authors
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M.Rovoli,
T.Thireou,
Y.Choiset,
T.Haertlé,
L.Sawyer,
E.Eliopoulos,
G.Kontopidis.
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Ref.
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Int J Biol Macromol, 2018,
118,
296-303.
[DOI no: ]
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PubMed id
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Abstract
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The milk protein β-lactoglobulin has been widely studied since its discovery,
both as a purified protein and in mixtures with other milk proteins, where its
effect on the processing properties is of importance to the dairy industry. The
protein can bind a variety of small hydrophobic molecules, which may allow its
use as an oral delivery vehicle. In the present study we have examined the
binding of odd-numbered fatty acids by isothermal calorimetry (ITC), X-ray
crystallography and computer modelling to provide a clearer picture of the
extent and variability of the central binding pocket. The Kd values for the
fatty acids C13, C15, C16, C17 and C19 as determined by ITC are 1.93, 2.91,
3.05, 4.11 and 8.67 × 10-7 M, respectively. The molecular
structures revealed the ligands bound in the central cavity with generally well
ordered lipophilic tails but significant positional variation at the carboxyl
group end. In silico docking analyses identified the lipophilic interactions
within the central cavity as the main driving force for binding with
electrostatic interactions and H-bonds playing a minor role.
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