4AHA

Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with fucosylated monosaccharides (Fuc1-2Gal, Fuc1- 3GlcNAc, Fuc1-4GlcNAc and Fuc1-6GlcNAc)

4AHA の概要

• エントリーDOI: 10.2210/pdb4aha/pdb
• 関連するPDBエントリー: 4AGI 4AGT 4AH4 4AH5
• 分子名称: Fucose-specific lectin, alpha-L-fucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose, ... (4 entities in total)
• 機能のキーワード: sugar binding protein
• 由来する生物種: ASPERGILLUS FUMIGATUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72007.57

構造登録者

Houser, J.,Komarek, J.,Kostlanova, N.,Lahmann, M.,Cioci, G.,Varrot, A.,Imberty, A.,Wimmerova, M. (登録日: 2012-02-06, 公開日: 2013-02-20, 最終更新日: 2023-12-20)

主引用文献

Houser, J.,Komarek, J.,Cioci, G.,Varrot, A.,Imberty, A.,Wimmerova, M.
Structural Insights Into Aspergillus Fumigatus Lectin Specificity: Afl Binding Sites are Functionally Non-Equivalent
Acta Crystallogr.,Sect.D, 71:442-, 2015

PubMed Abstract: The Aspergillus fumigatus lectin AFL was recently described as a new member of the AAL lectin family. As a lectin from an opportunistic pathogen, it might play an important role in the interaction of the pathogen with the human host. A detailed study of structures of AFL complexed with several monosaccharides and oligosaccharides, including blood-group epitopes, was combined with affinity data from SPR and discussed in the context of previous findings. Its six binding sites are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition. AFL displays a high affinity in the micromolar range towards oligosaccharides which were detected in plants and also those bound on the human epithelia. All of these results indicate AFL to be a complex member of the lectin family and a challenging target for future medical research and, owing to its binding properties, a potentially useful tool in specific biotechnological applications.

PubMed: 25760594
DOI: 10.1107/S1399004714026595

実験手法

X-RAY DIFFRACTION (2.2 Å)