Ficolin: Difference between revisions

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{{STRUCTURE_2j64|  PDB=2j64 | SIZE=400| SCENE= |right|CAPTION=Human H-ficolin binding domain trimer complex with Ca+2 ion, [[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]]) '>


'''Ficolin''' (Fic) are defense proteins which belong to the innate immune system and recognize carbohydrate molecules.  3 ficolins were identified in humans L-Fic, H-Fic and M-Fic.
== Function ==


{{TOC limit|limit=2}}
'''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>.


== 3D Structures of Ficoln ==
== Disease ==


===H-ficolin===
Fn may play a role in inflammatory diseases, apoptosis, lupus, preeclampsia and IgA nephropathy<ref>PMID:19025118</ref>.


[[2j64]] - hH-Fic binding domain - human<br />
== Structural highlights ==
[[2j5z]] - hH-Fic binding domain + galactose<br />
[[2j60]] - hH-Fic binding domain + fucose<br />
[[2j61]] - hH-Fic binding domain + acetyl-glucosamine<br />


===L-ficolin===
<scene name='46/466464/Cv/4'>Human H-ficolin binding domain trimer</scene>.


[[2j3g]] - hL-Fic binding domain<br />
<scene name='46/466464/Cv/5'>Ca coordination site</scene> (PDB code [[2j64]]).<ref>PMID:17215869</ref> Water molecules shown as red spheres.
[[2j0g]] – hL-Fic binding domain + N-acetyl-mannosamine<br />
</StructureSection>
[[2j0h]] - hL-Fic binding domain + acetylcholine<br />
== 3D Structures of Ficolin ==
[[2j0y]] - hL-Fic binding domain + glucan<br />
[[2j1g]], [[2j2p]] - hL-Fic binding domain + acetylcysteine<br />
[[2j3f]] - hL-Fic binding domain + galactosamine<br />
[[2j3o]] - hL-Fic binding domain + acetyl-glucosamine<br />
[[2j3u]] - hL-Fic binding domain + galactose<br />


===M-ficolin===
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|


[[2d39]] – hM-Fic fibrinogen-like domain<br />
*H-ficolin
[[2wnp]] - hM-Fic fibrinogen-like domain (mutant) <br />
[[2jhh]], [[2jhm]] – hM-Fic C terminal<br />
[[2jhi]] - hL-Mic C terminal + acetyl-galactosamine<br />
[[2jhk]] - hL-Mic C terminal + acetyl-glucosamine<br />
[[2jhl]] - hL-Mic C terminal + sialic acid


**[[2j64]] - hH-Fic binding domain - human<br />
**[[2j5z]] - hH-Fic binding domain + galactose<br />
**[[2j60]] - hH-Fic binding domain + fucose<br />
**[[2j61]] - hH-Fic binding domain + acetyl-glucosamine<br />


*L-ficolin


**[[2j3g]], [[4r9t]] - hL-Fic binding domain<br />
**[[2j0g]] – hL-Fic binding domain + N-acetyl-mannosamine<br />
**[[2j0h]] - hL-Fic binding domain + acetylcholine<br />
**[[4nyt]] - hL-Fic binding domain + phosphocholine<br />
**[[2j0y]] - hL-Fic binding domain + glucan<br />
**[[2j1g]], [[2j2p]] - hL-Fic binding domain + acetylcysteine<br />
**[[2j3f]] - hL-Fic binding domain + galactosamine<br />
**[[2j3o]] - hL-Fic binding domain + acetyl-glucosamine<br />
**[[4r9j]] - hL-Fic binding domain + glucosamine sulfate<br />
**[[2j3u]] - hL-Fic binding domain + galactose<br />
*M-ficolin
**[[2d39]] – hM-Fic fibrinogen-like domain<br />
**[[2wnp]] - hM-Fic fibrinogen-like domain (mutant) <br />
**[[2jhh]], [[2jhm]] – hM-Fic C terminal<br />
**[[2jhi]] - hL-Mic C terminal + acetyl-galactosamine<br />
**[[2jhk]] - hL-Mic C terminal + acetyl-glucosamine<br />
**[[2jhl]] - hL-Mic C terminal + sialic acid
}}
== References ==
<references/>





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