2J64

H-ficolin

2J64 の概要

• エントリーDOI: 10.2210/pdb2j64/pdb
• 関連するPDBエントリー: 1LA5 2J5Z 2J60
• 分子名称: FICOLIN-3, CALCIUM ION (3 entities in total)
• 機能のキーワード: lectin, collagen, immunology, glycoprotein, immune system, hydroxylation
• 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: 75461.66

構造登録者

Garlatti, V.,Gaboriaud, C. (登録日: 2006-09-25, 公開日: 2007-01-23, 最終更新日: 2024-11-20)

主引用文献

Garlatti, V.,Belloy, N.,Martin, L.,Lacroix, M.,Matsushita, M.,Endo, Y.,Fujita, T.,Fontecilla-Camps, J.C.,Arlaud, G.J.,Thielens, N.M.,Gaboriaud, C.
Structural Insights Into the Innate Immune Recognition Specificities of L- and H-Ficolins.
Embo J., 26:623-, 2007

PubMed Abstract: Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L- and H-ficolins are soluble oligomeric defence proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains. The X-ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 A, respectively. Both domains have three-lobed structures with clefts separating the distal parts of the protomers. Ca(2+) ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc-binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L-ficolin, three additional binding sites (S2-S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3-beta-D-glucan, as found on microbial or apoptotic surfaces.

PubMed: 17215869
DOI: 10.1038/SJ.EMBOJ.7601500

実験手法

X-RAY DIFFRACTION (2.2 Å)