Ficolin: Difference between revisions

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<scene name='46/466464/Cv/2'>Human H-ficolin binding domain trimer</scene>.
<scene name='46/466464/Cv/2'>Human H-ficolin binding domain trimer</scene>.


<scene name='46/466464/Cv/3'>Ca coordination site</scene> (PDB code [[2j64]]).<ref>PMID:17215869</ref>
<scene name='46/466464/Cv/3'>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 ==

Revision as of 14:17, 21 February 2016


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

.

(PDB code 2j64).[3] 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 21-February-2016


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. Zhang XL, Ali MA. Ficolins: structure, function and associated diseases. Adv Exp Med Biol. 2008;632:105-15. PMID:19025118
  3. 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