1B0O

BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE Z

1B0O の概要

• エントリーDOI: 10.2210/pdb1b0o/pdb
• 分子名称: BETA-LACTOGLOBULIN, PALMITIC ACID (3 entities in total)
• 機能のキーワード: lipocalin, milk whey protein, bovine, palmitate-binding
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18557.60

構造登録者

Wu, S.-Y.,Sawyer, L. (登録日: 1998-11-11, 公開日: 1999-02-02, 最終更新日: 2024-10-30)

主引用文献

Wu, S.Y.,Perez, M.D.,Puyol, P.,Sawyer, L.
beta-lactoglobulin binds palmitate within its central cavity.
J.Biol.Chem., 274:170-174, 1999

PubMed Abstract: Bovine beta-lactoglobulin (beta-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, beta-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 beta-strands that are typical of the lipocalins. We have now cocrystallized beta-Lg with palmitic acid, and the refined structure (R = 0.204, Rfree = 0.240 for 6,888 reflections to 2.5-A 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 beta-Lg.

PubMed: 9867826
DOI: 10.1074/jbc.274.1.170

実験手法

X-RAY DIFFRACTION (2.5 Å)