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Function
Ficolin (Fic) are defense proteins which belong to the innate immune system and recognize carbohydrate molecules[1]. 3 ficolins were identified in humans L-Fic or ficolin-2, H-Fic or ficolin-3 and M-Fic or ficolin-1.
Disease
Fn may play a role in inflammatory diseases, apoptosis, lupus, preeclampsia and IgA nephropathy[2].
Structural highlights
Human H-ficolin binding domain trimer.
Ca coordination site (PDB code 2j64).[3]
- ↑ Lu J, Le Y. Ficolins and the fibrinogen-like domain. Immunobiology. 1998 Aug;199(2):190-9. PMID:9777405 doi:https://dx.doi.org/10.1016/S0171-2985(98)80026-0
- ↑ Zhang XL, Ali MA. Ficolins: structure, function and associated diseases. Adv Exp Med Biol. 2008;632:105-15. PMID:19025118
- ↑ Garlatti V, Belloy N, Martin L, Lacroix M, Matsushita M, Endo Y, Fujita T, Fontecilla-Camps JC, Arlaud GJ, Thielens NM, Gaboriaud C. Structural insights into the innate immune recognition specificities of L- and H-ficolins. EMBO J. 2007 Jan 24;26(2):623-33. Epub 2007 Jan 11. PMID:17215869
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3D Structures of Ficolin
Updated on 21-February-2016
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- H-ficolin
- 2j64 - hH-Fic binding domain - human
- 2j5z - hH-Fic binding domain + galactose
- 2j60 - hH-Fic binding domain + fucose
- 2j61 - hH-Fic binding domain + acetyl-glucosamine
- L-ficolin
- 2j3g, 4r9t - hL-Fic binding domain
- 2j0g – hL-Fic binding domain + N-acetyl-mannosamine
- 2j0h - hL-Fic binding domain + acetylcholine
- 4nyt - hL-Fic binding domain + phosphocholine
- 2j0y - hL-Fic binding domain + glucan
- 2j1g, 2j2p - hL-Fic binding domain + acetylcysteine
- 2j3f - hL-Fic binding domain + galactosamine
- 2j3o - hL-Fic binding domain + acetyl-glucosamine
- 4r9j - hL-Fic binding domain + glucosamine sulfate
- 2j3u - hL-Fic binding domain + galactose
- M-ficolin
- 2d39 – hM-Fic fibrinogen-like domain
- 2wnp - hM-Fic fibrinogen-like domain (mutant)
- 2jhh, 2jhm – hM-Fic C terminal
- 2jhi - hL-Mic C terminal + acetyl-galactosamine
- 2jhk - hL-Mic C terminal + acetyl-glucosamine
- 2jhl - hL-Mic C terminal + sialic acid
References
