2J0G

L-ficolin complexed to N-acetyl-mannosamine

Summary for 2J0G

• Entry DOI: 10.2210/pdb2j0g/pdb
• Related: 2J0H 2J0Y 2J1G 2J2P 2J3F 2J3G 2J3O 2J3U 2J61
• Descriptor: FICOLIN-2, alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: lectin, glycoprotein, innate immunity, fibrinogen-like domain, collagen, immunology, lectin-like, pattern- recognition-protein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 6
• Total formula weight: 151308.87

Authors

Garlatti, V.,Gaboriaud, C. (deposition date: 2006-08-03, release date: 2007-01-23, Last modification date: 2020-07-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.85 Å)