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Ficolin

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<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]]) '>
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== Function ==
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'''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'''.
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== Disease ==
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'''Ficolin''' (Fic) are defense proteins which belong to the innate immune system and recognize carbohydrate molecules<ref>PMID:8747466</ref>. 3 ficolins were identified in humans L-Fic, H-Fic and M-Fic.
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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

Human H-ficolin binding domain trimer complex with Ca+2 ion (PDB code 2j64)

Drag the structure with the mouse to rotate

3D Structures of Ficolin

Updated on 22-January-2016


References

  1. 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
  2. Zhang XL, Ali MA. Ficolins: structure, function and associated diseases. Adv Exp Med Biol. 2008;632:105-15. PMID:19025118

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