2JN3

NMR structure of cl-BABP complexed to chenodeoxycholic acid

2JN3 の概要

• エントリーDOI: 10.2210/pdb2jn3/pdb
• NMR情報: BMRB: 15084
• 分子名称: Fatty acid-binding protein, liver, CHENODEOXYCHOLIC ACID (2 entities in total)
• 機能のキーワード: bile acids, lipid binding protein
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Cytoplasm: P80226
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14885.32

構造登録者

Eliseo, T.,Ragona, L.,Catalano, M.,Assfalf, M.,Paci, M.,Zetta, L.,Molinari, H.,Cicero, D.O. (登録日: 2006-12-22, 公開日: 2007-07-03, 最終更新日: 2023-12-20)

主引用文献

Eliseo, T.,Ragona, L.,Catalano, M.,Assfalg, M.,Paci, M.,Zetta, L.,Molinari, H.,Cicero, D.O.
Structural and dynamic determinants of ligand binding in the ternary complex of chicken liver bile acid binding protein with two bile salts revealed by NMR
Biochemistry, 46:12557-12567, 2007

PubMed Abstract: Bile acids are physiological detergents facilitating absorption, transport, and distribution of lipid-soluble vitamins and dietary fats;they also play a role as signaling molecules that activate nuclear receptors and regulate cholesterol metabolism. Bile acid circulation is mediated by bile acid binding proteins (BABPs), and a detailed structural study of the complex of BABPs with bile salts has become a key issue for the complete understanding of the role of these proteins and their involvement in cholesterol homeostasis. The solution structure here reported describes, at variance with previously determined singly ligated structures, a BABP in a ternary complex with two bile acid molecules, obtained by employing a variety of NMR experiments. Exchange processes between the two bound chenodeoxycholate molecules as well as the more superficial ligand and the free pool have been detected through ROESY and diffusion experiments. Significant backbone flexibility has been observed in regions located at the protein open end, facilitating bile salts exchange. A detailed description of the protonation states and tautomeric forms of histidines strongly supports the view that histidine protonation modulates backbone flexibility and regulates ligand binding. This structure opens the way to targeted site-directed mutagenesis and interaction studies to investigate both binding and nuclear localization mechanisms.

PubMed: 17929837
DOI: 10.1021/bi7013085

実験手法

SOLUTION NMR