7KOT

Energetic and structural effects of the Tanford transition on the ligand recognition of bovine Beta-lactoglobulin

7KOT の概要

• エントリーDOI: 10.2210/pdb7kot/pdb
• 分子名称: Beta-lactoglobulin, DODECYL SULFATE (3 entities in total)
• 機能のキーワード: bovine beta-lactoglobulin, lipocalin, tanford transition, structural energetics, transport protein
• 由来する生物種: Bos taurus (Bovine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18567.57

構造登録者

Rodriguez-Hernandez, A.,Rodriguez-Romero, A. (登録日: 2020-11-09, 公開日: 2021-01-27, 最終更新日: 2024-11-20)

主引用文献

Labra-Nunez, A.,Cofas-Vargas, L.F.,Gutierrez-Magdaleno, G.,Gomez-Velasco, H.,Rodriguez-Hernandez, A.,Rodriguez-Romero, A.,Garcia-Hernandez, E.
Energetic and structural effects of the Tanford transition on ligand recognition of bovine beta-lactoglobulin.
Arch.Biochem.Biophys., 699:108750-108750, 2021

PubMed Abstract: Bovine β-lactoglobulin, an abundant protein in whey, is a promising nanocarrier for peroral administration of drug-like hydrophobic molecules, a process that involves transit through the different acidic conditions of the human digestive tract. Among the several pH-induced conformational rearrangements that this lipocalin undergoes, the Tanford transition is particularly relevant. This transition, which occurs with a midpoint around neutral pH, involves a conformational change of the E-F loop that regulates accessibility to the primary binding site. The effect of this transition on the ligand binding properties of this protein has scarcely been explored. In this study, we carried out an energetic and structural characterization of β-lactoglobulin molecular recognition at pH values above and below the zone in which the Tanford transition occurs. The combined analysis of crystallographic, calorimetric, and molecular dynamics data sheds new light on the interplay between self-association, ligand binding, and the Tanford pre- and post-transition conformational states, revealing novel aspects underlying the molecular recognition mechanism of this enigmatic lipocalin.

PubMed: 33421379
DOI: 10.1016/j.abb.2020.108750

実験手法

X-RAY DIFFRACTION (1.74 Å)