2J2P
L-ficolin complexed to N-acetyl-cystein (150mM)
Summary for 2J2P
| Entry DOI | 10.2210/pdb2j2p/pdb |
| Related | 2J0G 2J0H 2J0Y 2J1G 2J3F 2J3G 2J3O 2J3U 2J61 |
| Descriptor | FICOLIN-2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | glycoprotein, ficrinogen-like, innate immunity, pattern recognition protein, lectin, collagen, immunology, lectin- like |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 6 |
| Total formula weight | 151766.87 |
| Authors | Garlatti, V.,Gaboriaud, C. (deposition date: 2006-08-17, release date: 2007-01-23, Last modification date: 2024-11-20) |
| 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 Cited by 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: 17215869DOI: 10.1038/SJ.EMBOJ.7601500 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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