4R9J

L-ficolin complexed to glucosamine-6-sulfate

4R9J の概要

• エントリーDOI: 10.2210/pdb4r9j/pdb
• 関連するPDBエントリー: 2J0G 2J0H 2J0Y 2J3O 4R9T
• 分子名称: Ficolin-2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (8 entities in total)
• 機能のキーワード: fibrinogen-like domain, innate immunity, pattern recognition protein, lectin, immunology, lectin-like, sugar binding protein, plasma, extracellular
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 76088.95

構造登録者

Laffly, E.,Lacroix, M.,Martin, L.,Vassal-Stermann, E.,Thielens, N.,Gaboriaud, C. (登録日: 2014-09-05, 公開日: 2014-11-05, 最終更新日: 2024-10-30)

主引用文献

Laffly, E.,Lacroix, M.,Martin, L.,Vassal-Stermann, E.,Thielens, N.M.,Gaboriaud, C.
Human ficolin-2 recognition versatility extended: An update on the binding of ficolin-2 to sulfated/phosphated carbohydrates.
Febs Lett., 588:4694-4700, 2014

PubMed Abstract: Ficolin-2 has been reported to bind to DNA and heparin, but the mechanism involved has not been thoroughly investigated. X-ray studies of the ficolin-2 fibrinogen-like domain in complex with several new ligands now show that sulfate and phosphate groups are prone to bind to the S3 binding site of the protein. Composed of Arg132, Asp133, Thr136 and Lys221, the S3 site was previously shown to mainly bind N-acetyl groups. Furthermore, DNA and heparin compete for binding to ficolin-2. Mutagenesis studies reveal that Arg132, and to a lesser extent Asp133, are important for this binding property. The versatility of the S3 site in binding N-acetyl, sulfate and phosphate groups is discussed through comparisons with homologous fibrinogen-like recognition proteins.

PubMed: 25447524
DOI: 10.1016/j.febslet.2014.10.042

実験手法

X-RAY DIFFRACTION (2.1 Å)