1sl6
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1sl6' size='340' side='right'caption='[[1sl6]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='1sl6' size='340' side='right'caption='[[1sl6]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1sl6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1sl6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SL6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PRD_900120:Lewis+X+antigen,+alpha+anomer'>PRD_900120</scene></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=1sl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sl6 OCA], [https://pdbe.org/1sl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sl6 RCSB], [https://www.ebi.ac.uk/pdbsum/1sl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sl6 ProSAT]</span></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=1sl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sl6 OCA], [https://pdbe.org/1sl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sl6 RCSB], [https://www.ebi.ac.uk/pdbsum/1sl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sl6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CLC4M_HUMAN CLC4M_HUMAN] Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus.<ref>PMID:11257134</ref> <ref>PMID:11226297</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 17: | Line 20: | ||
</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=1sl6 ConSurf]. | </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=1sl6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Both the dendritic cell receptor DC-SIGN and the closely related endothelial cell receptor DC-SIGNR bind human immunodeficiency virus and enhance infection. However, biochemical and structural comparison of these receptors now reveals that they have very different physiological functions. By screening an extensive glycan array, we demonstrated that DC-SIGN and DC-SIGNR have distinct ligand-binding properties. Our structural and mutagenesis data explain how both receptors bind high-mannose oligosaccharides on enveloped viruses and why only DC-SIGN binds blood group antigens, including those present on microorganisms. DC-SIGN mediates endocytosis, trafficking as a recycling receptor and releasing ligand at endosomal pH, whereas DC-SIGNR does not release ligand at low pH or mediate endocytosis. Thus, whereas DC-SIGN has dual ligand-binding properties and functions both in adhesion and in endocytosis of pathogens, DC-SIGNR binds a restricted set of ligands and has only the properties of an adhesion receptor. | ||
| - | |||
| - | Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR.,Guo Y, Feinberg H, Conroy E, Mitchell DA, Alvarez R, Blixt O, Taylor ME, Weis WI, Drickamer K Nat Struct Mol Biol. 2004 Jul;11(7):591-8. Epub 2004 Jun 13. PMID:15195147<ref>PMID:15195147</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1sl6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Alvarez | + | [[Category: Alvarez R]] |
| - | [[Category: Blixt | + | [[Category: Blixt O]] |
| - | [[Category: Conroy | + | [[Category: Conroy E]] |
| - | [[Category: Drickamer | + | [[Category: Drickamer K]] |
| - | [[Category: Feinberg | + | [[Category: Feinberg H]] |
| - | [[Category: Guo | + | [[Category: Guo Y]] |
| - | [[Category: Mitchell | + | [[Category: Mitchell DA]] |
| - | [[Category: Taylor | + | [[Category: Taylor ME]] |
| - | [[Category: Weis | + | [[Category: Weis WI]] |
| - | + | ||
| - | + | ||
| - | + | ||
Revision as of 08:32, 1 May 2024
Crystal Structure of a fragment of DC-SIGNR (containg the carbohydrate recognition domain and two repeats of the neck) complexed with Lewis-x.
| |||||||||||
Categories: Homo sapiens | Large Structures | Alvarez R | Blixt O | Conroy E | Drickamer K | Feinberg H | Guo Y | Mitchell DA | Taylor ME | Weis WI
