3NQ9

Bovine beta-lactoglobulin complex with caprylic acid

3NQ9 の概要

• エントリーDOI: 10.2210/pdb3nq9/pdb
• 関連するPDBエントリー: 3NPO 3NQ3
• 分子名称: Beta-lactoglobulin, OCTANOIC ACID (CAPRYLIC ACID), CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: beta-lactoglobulin, lipocalin, bovine milk, caprylic acid, octanoic acid, fatty acid, transport protein
• 由来する生物種: Bos taurus (Bovine)
• 細胞内の位置: Secreted: P02754
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18480.84

構造登録者

Loch, J.I.,Lewinski, K. (登録日: 2010-06-29, 公開日: 2010-07-14, 最終更新日: 2024-11-13)

主引用文献

Loch, J.I.,Polit, A.,Gorecki, A.,Bonarek, P.,Kurpiewska, K.,Dziedzicka-Wasylewska, M.,Lewinski, K.
Two modes of fatty acid binding to bovine beta-lactoglobulin-crystallographic and spectroscopic studies
J.Mol.Recognit., 24:341-349, 2011

PubMed Abstract: Lactoglobulin is a natural protein present in bovine milk and common component of human diet, known for binding with high affinity wide range of hydrophobic compounds, among them fatty acids 12-20 carbon atoms long. Shorter fatty acids were reported as not binding to β-lactoglobulin. We used X-ray crystallography and fluorescence spectroscopy to show that lactoglobulin binds also 8- and 10-carbon caprylic and capric acids, however with lower affinity. The determined apparent association constant for lactoglobulin complex with caprylic acid is 10.8 ± 1.7 × 10(3) M(-1), while for capric acid is 6.0 ± 0.5 × 10(3) M(-1). In crystal structures determined with resolution 1.9 Å the caprylic acid is bound in upper part of central calyx near polar residues located at CD loop, while the capric acid is buried deeper in the calyx bottom and does not interact with polar residues at CD loop. In both structures, water molecule hydrogen-bonded to carboxyl group of fatty acid is observed. Different location of ligands in the binding site indicates that competition between polar and hydrophobic interactions is an important factor determining position of the ligand in β-barrel.

PubMed: 21360616
DOI: 10.1002/jmr.1084

実験手法

X-RAY DIFFRACTION (1.9 Å)