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2j60

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Revision as of 06:52, 11 July 2018

H-ficolin complexed to D-fucose

Structural highlights

2j60 is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1la5, 2j5z, 2j61
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[FCN3_HUMAN] Defects in FCN3 are the cause of ficolin 3 deficiency (FCN3D) [MIM:613860]. FCN3D is a disorder characterized by immunodeficiency, recurrent infections, brain abscesses and recurrent warts on the fingers. Affected individuals have normal levels of lymphocytes, normal T-cell responses, and normal antibodies, but a selective deficient antibody response to pneumococcal polysaccharide vaccine.^[1]

Function

[FCN3_HUMAN] May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L- and H-ficolins are soluble oligomeric defence proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains. The X-ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 A, respectively. Both domains have three-lobed structures with clefts separating the distal parts of the protomers. Ca(2+) ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc-binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L-ficolin, three additional binding sites (S2-S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3-beta-D-glucan, as found on microbial or apoptotic surfaces.

Structural insights into the innate immune recognition specificities of L- and H-ficolins.,Garlatti V, Belloy N, Martin L, Lacroix M, Matsushita M, Endo Y, Fujita T, Fontecilla-Camps JC, Arlaud GJ, Thielens NM, Gaboriaud C EMBO J. 2007 Jan 24;26(2):623-33. Epub 2007 Jan 11. PMID:17215869^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Munthe-Fog L, Hummelshoj T, Honore C, Madsen HO, Permin H, Garred P. Immunodeficiency associated with FCN3 mutation and ficolin-3 deficiency. N Engl J Med. 2009 Jun 18;360(25):2637-44. doi: 10.1056/NEJMoa0900381. PMID:19535802 doi:10.1056/NEJMoa0900381
↑ Matsushita M, Kuraya M, Hamasaki N, Tsujimura M, Shiraki H, Fujita T. Activation of the lectin complement pathway by H-ficolin (Hakata antigen). J Immunol. 2002 Apr 1;168(7):3502-6. PMID:11907111
↑ 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

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j60"

@@ Line 1: / Line 1: @@
-==H-FICOLIN COMPLEXED TO D-FUCOSE==
+==H-ficolin complexed to D-fucose==
 <StructureSection load='2j60' size='340' side='right' caption='[[2j60]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABE:ABEQUOSE'>ABE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1la5|1la5]], [[2j5z|2j5z]], [[2j61|2j61]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j60 OCA], [http://pdbe.org/2j60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j60 RCSB], [http://www.ebi.ac.uk/pdbsum/2j60 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j60 OCA], [http://pdbe.org/2j60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j60 RCSB], [http://www.ebi.ac.uk/pdbsum/2j60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j60 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j6/2j60_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j6/2j60_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2j60

From Proteopedia

Revision as of 06:52, 11 July 2018

H-ficolin complexed to D-fucose

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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