1OOG

Complex of Drosophila odorant binding protein LUSH with propanol

1OOG の概要

• エントリーDOI: 10.2210/pdb1oog/pdb
• 関連するPDBエントリー: 1OOF 1OOH 1OOI
• 分子名称: odorant binding protein LUSH, ACETATE ION, N-PROPANOL, ... (4 entities in total)
• 機能のキーワード: lush, alcohol, odorant binding, transport protein
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Secreted: O02372
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28787.38

構造登録者

Kruse, S.W.,Zhao, R.,Smith, D.P.,Jones, D.N.M. (登録日: 2003-03-03, 公開日: 2003-09-02, 最終更新日: 2024-10-16)

主引用文献

Kruse, S.W.,Zhao, R.,Smith, D.P.,Jones, D.N.M.
Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster
Nat.Struct.Biol., 10:694-700, 2003

PubMed Abstract: We have solved the high-resolution crystal structures of the Drosophila melanogaster alcohol-binding protein LUSH in complex with a series of short-chain n-alcohols. LUSH is the first known nonenzyme protein with a defined in vivo alcohol-binding function. The structure of LUSH reveals a set of molecular interactions that define a specific alcohol-binding site. A group of amino acids, Thr57, Ser52 and Thr48, form a network of concerted hydrogen bonds between the protein and the alcohol that provides a structural motif to increase alcohol-binding affinity at this site. This motif seems to be conserved in a number of mammalian ligand-gated ion channels that are directly implicated in the pharmacological effects of alcohol. Further, these sequences are found in regions of ion channels that are known to confer alcohol sensitivity. We suggest that the alcohol-binding site in LUSH represents a general model for alcohol-binding sites in proteins.

PubMed: 12881720
DOI: 10.1038/nsb960

実験手法

X-RAY DIFFRACTION (1.45 Å)