Ficolin: Difference between revisions

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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='46/466464/Cv/1' caption='Human H-ficolin binding domain trimer complex with Ca+2 ion (PDB code [[2j64]]) '>


== Function ==
== 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'''.
'''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'''.
*'''Fiicolin-1''' or '''M-ficolin''' is a pattern recognition molecule of the complement system expressed in myeloid cells<ref>PMID:18343499</ref>.


== Disease ==
== Disease ==


Fn may play a role in inflammatory diseases, apoptosis, lupus, preeclampsia and IgA nephropathy<ref>PMID:19025118</ref>.
Fn may play a role in inflammatory diseases, apoptosis, lupus, preeclampsia and IgA nephropathy<ref>PMID:19025118</ref>.
== Structural highlights ==
<scene name='46/466464/Cv/4'>Human H-ficolin binding domain trimer</scene>.
<scene name='46/466464/Cv/5'>Ca coordination site</scene> (PDB code [[2j64]]).<ref>PMID:17215869</ref> Water molecules shown as red spheres.
</StructureSection>
</StructureSection>
== 3D Structures of Ficolin ==
== 3D Structures of Ficolin ==

Latest revision as of 11:00, 23 June 2024


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.

  • Fiicolin-1 or M-ficolin is a pattern recognition molecule of the complement system expressed in myeloid cells[2].

Disease

Fn may play a role in inflammatory diseases, apoptosis, lupus, preeclampsia and IgA nephropathy[3].

Structural highlights

.

(PDB code 2j64).[4] Water molecules shown as red spheres.

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 Ficolin3D Structures of Ficolin

Updated on 23-June-2024


ReferencesReferences

  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. Honoré C, Rørvig S, Munthe-Fog L, Hummelshøj T, Madsen HO, Borregaard N, Garred P. The innate pattern recognition molecule Ficolin-1 is secreted by monocytes/macrophages and is circulating in human plasma. Mol Immunol. 2008 May;45(10):2782-9. PMID:18343499 doi:10.1016/j.molimm.2008.02.005
  3. Zhang XL, Ali MA. Ficolins: structure, function and associated diseases. Adv Exp Med Biol. 2008;632:105-15. PMID:19025118
  4. 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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Michal Harel, Alexander Berchansky