5H9K

Crystal of a leukotriene-binding salivary lipocalin

5H9K の概要

• エントリーDOI: 10.2210/pdb5h9k/pdb
• 分子名称: Lipocalin AI-4 (2 entities in total)
• 機能のキーワード: lipocalin, rhodnius prolixus, ligand-binding, protein binding
• 由来する生物種: Rhodnius prolixus (Triatomid bug)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16904.71

構造登録者

Andersen, J.F.,Jablonka, W. (登録日: 2015-12-28, 公開日: 2016-05-11, 最終更新日: 2024-11-20)

主引用文献

Jablonka, W.,Pham, V.,Nardone, G.,Gittis, A.,Silva-Cardoso, L.,Atella, G.C.,Ribeiro, J.M.,Andersen, J.F.
Structure and Ligand-Binding Mechanism of a Cysteinyl Leukotriene-Binding Protein from a Blood-Feeding Disease Vector.
Acs Chem.Biol., 11:1934-1944, 2016

PubMed Abstract: Blood-feeding disease vectors mitigate the negative effects of hemostasis and inflammation through the binding of small-molecule agonists of these processes by salivary proteins. In this study, a lipocalin protein family member (LTBP1) from the saliva of Rhodnius prolixus, a vector of the pathogen Trypanosoma cruzi, is shown to sequester cysteinyl leukotrienes during feeding to inhibit immediate inflammatory responses. Calorimetric binding experiments showed that LTBP1 binds leukotrienes C4 (LTC4), D4 (LTD4), and E4 (LTE4) but not biogenic amines, adenosine diphosphate, or other eicosanoid compounds. Crystal structures of ligand-free LTBP1 and its complexes with LTC4 and LTD4 reveal a conformational change during binding that brings Tyr114 into close contact with the ligand. LTC4 is cleaved in the complex, leaving free glutathione and a C20 fatty acid. Chromatographic analysis of bound ligands showed only intact LTC4, suggesting that cleavage could be radiation-mediated.

PubMed: 27124118
DOI: 10.1021/acschembio.6b00032

実験手法

X-RAY DIFFRACTION (1.352 Å)