2j0g: Difference between revisions
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== | ==L-ficolin complexed to N-acetyl-mannosamine== | ||
<StructureSection load='2j0g' size='340' side='right'caption='[[2j0g]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
[[ | == Structural highlights == | ||
[[ | <table><tr><td colspan='2'>[[2j0g]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J0G FirstGlance]. <br> | ||
[[ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BM3:2-(ACETYLAMINO)-2-DEOXY-ALPHA-D-MANNOPYRANOSE'>BM3</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
[[ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2j0h|2j0h]], [[2j0y|2j0y]], [[2j1g|2j1g]], [[2j2p|2j2p]], [[2j3f|2j3f]], [[2j3g|2j3g]], [[2j3o|2j3o]], [[2j3u|2j3u]], [[2j61|2j61]]</div></td></tr> | ||
[[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0g OCA], [https://pdbe.org/2j0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j0g RCSB], [https://www.ebi.ac.uk/pdbsum/2j0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j0g ProSAT]</span></td></tr> | ||
[[ | </table> | ||
[[ | == Evolutionary Conservation == | ||
[[ | [[Image:Consurf_key_small.gif|200px|right]] | ||
[[ | Check<jmol> | ||
[[ | <jmolCheckbox> | ||
[[ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j0/2j0g_consurf.spt"</scriptWhenChecked> | ||
[ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
[[ | <text>to colour the structure by Evolutionary Conservation</text> | ||
[ | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j0g ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:17215869</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2j0g" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ficolin|Ficolin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Gaboriaud, C]] | |||
[[Category: Garlatti, V]] | |||
[[Category: Collagen]] | |||
[[Category: Fibrinogen-like domain]] | |||
[[Category: Glycoprotein]] | |||
[[Category: Immunology]] | |||
[[Category: Innate immunity]] | |||
[[Category: Lectin]] | |||
[[Category: Lectin-like]] | |||
[[Category: Pattern- recognition-protein]] | |||
Latest revision as of 14:23, 31 March 2021
L-ficolin complexed to N-acetyl-mannosamineL-ficolin complexed to N-acetyl-mannosamine
Structural highlights
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 PubMedInnate 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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