Ficolin
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | |||
<StructureSection load='2j64' size='350' side='right' scene='' caption='Human H-ficolin binding domain trimer complex with Ca+2 ion (PDB code [[2j64]]) '> | <StructureSection load='2j64' size='350' side='right' scene='' caption='Human H-ficolin binding domain trimer complex with Ca+2 ion (PDB code [[2j64]]) '> | ||
| + | == Function == | ||
| + | |||
| + | '''Ficolin''' (Fic) are defense proteins which belong to the innate immune system and recognize carbohydrate molecules<ref>PMID:9777405</ref>. 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<ref>PMID:19025118</ref>. | |
</StructureSection> | </StructureSection> | ||
== 3D Structures of Ficolin == | == 3D Structures of Ficolin == | ||
Revision as of 14:45, 22 January 2016
| |||||||||||
3D Structures of Ficolin
Updated on 22-January-2016
References
- ↑ Lu J, Le Y. Ficolins and the fibrinogen-like domain. Immunobiology. 1998 Aug;199(2):190-9. PMID:9777405 doi:http://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
