3OBL

Crystal structure of the potent anti-HIV cyanobacterial lectin from Oscillatoria Agardhii

3OBL の概要

• エントリーDOI: 10.2210/pdb3obl/pdb
• 分子名称: Lectin, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID (3 entities in total)
• 機能のキーワード: novel beta barrel fold, anti-hiv lectin, high mannose glycans, sugar binding protein
• 由来する生物種: Planktothrix agardhii (Oscillatoria agardhii)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28746.78

構造登録者

Koharudin, L.M.I.,Furey, W.,Gronenborn, A.M. (登録日: 2010-08-06, 公開日: 2010-10-20, 最終更新日: 2024-02-21)

主引用文献

Koharudin, L.M.,Furey, W.,Gronenborn, A.M.
Novel fold and carbohydrate specificity of the potent anti-HIV cyanobacterial lectin from Oscillatoria agardhii.
J.Biol.Chem., 286:1588-1597, 2011

PubMed Abstract: Oscillatoria agardhii agglutinin (OAA) is a recently discovered cyanobacterial lectin that exhibits potent anti-HIV activity. Up to now, only its primary structure and carbohydrate binding data have been available. To elucidate the structural basis for the antiviral mechanism of OAA, we determined the structure of this lectin by x-ray crystallography at 1.2 Å resolution and mapped the specific carbohydrate recognition sites of OAA by NMR spectroscopy. The overall architecture of OAA comprises 10 β-strands that fold into a single, compact, β-barrel-like domain, creating a unique topology compared with all known protein structures in the Protein Data Bank. OAA sugar binding was tested against Man-9 and various disaccharide components of Man-9. Two symmetric carbohydrate-binding sites were located on the protein, and a preference for Manα(1-6)Man-linked sugars was found. Altogether, our structural results explain the antiviral activity OAA and add to the growing body of knowledge about antiviral lectins.

PubMed: 20961847
DOI: 10.1074/jbc.M110.173278

実験手法

X-RAY DIFFRACTION (1.2 Å)