2j0g: Difference between revisions

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[[Image:2j0g.gif|left|200px]]<br />
<applet load="2j0g" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2j0g, resolution 2.85&Aring;" />
'''L-FICOLIN COMPLEXED TO N-ACETYL-MANNOSAMINE'''<br />


==About this Structure==
==L-ficolin complexed to N-acetyl-mannosamine==
2J0G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MAN, CA and BM3 as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J0G OCA].  
<StructureSection load='2j0g' size='340' side='right'caption='[[2j0g]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
[[Category: Homo sapiens]]
== Structural highlights ==
[[Category: Single protein]]
<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>
[[Category: Gaboriaud, C.]]
</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>
[[Category: Garlatti, V.]]
<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>
[[Category: BM3]]
<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>
[[Category: CA]]
</table>
[[Category: MAN]]
== Evolutionary Conservation ==
[[Category: collagen]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: fibrinogen-like domain]]
Check<jmol>
[[Category: glycoprotein]]
  <jmolCheckbox>
[[Category: immunology]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j0/2j0g_consurf.spt"</scriptWhenChecked>
[[Category: innate immunity]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: lectin]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: lectin-like]]
  </jmolCheckbox>
[[Category: pattern- recognition-protein]]
</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.


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:50:08 2007''
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&reg;/PubMed&reg;, 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]]

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