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| | <StructureSection load='2ox8' size='340' side='right'caption='[[2ox8]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2ox8' size='340' side='right'caption='[[2ox8]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ox8]] is a 4 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=2OX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ox8]] is a 4 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=2OX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OX8 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRCL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2ox8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ox8 OCA], [https://pdbe.org/2ox8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ox8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ox8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ox8 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=2ox8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ox8 OCA], [https://pdbe.org/2ox8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ox8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ox8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ox8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/COL12_HUMAN COL12_HUMAN]] Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May also play a role in the clearance of amyloid beta in Alzheimer disease.<ref>PMID:11162630</ref> <ref>PMID:11564734</ref> <ref>PMID:12761161</ref> <ref>PMID:15845541</ref> <ref>PMID:16868960</ref>
| + | [https://www.uniprot.org/uniprot/COL12_HUMAN COL12_HUMAN] Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May also play a role in the clearance of amyloid beta in Alzheimer disease.<ref>PMID:11162630</ref> <ref>PMID:11564734</ref> <ref>PMID:12761161</ref> <ref>PMID:15845541</ref> <ref>PMID:16868960</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/2ox8_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/2ox8_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Drickamer, K]] | + | [[Category: Drickamer K]] |
| - | [[Category: Feinberg, H]] | + | [[Category: Feinberg H]] |
| - | [[Category: Taylor, M E]] | + | [[Category: Taylor ME]] |
| - | [[Category: Weis, W I]] | + | [[Category: Weis WI]] |
| - | [[Category: C-type lectin]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
COL12_HUMAN Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May also play a role in the clearance of amyloid beta in Alzheimer disease.[1] [2] [3] [4] [5]
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
The scavenger receptor C-type lectin (SRCL) is unique in the family of class A scavenger receptors, because in addition to binding sites for oxidized lipoproteins it also contains a C-type carbohydrate-recognition domain (CRD) that interacts with specific glycans. Both human and mouse SRCL are highly specific for the Lewis(x) trisaccharide, which is commonly found on the surfaces of leukocytes and some tumor cells. Structural analysis of the CRD of mouse SRCL in complex with Lewis(x) and mutagenesis show the basis for this specificity. The interaction between mouse SRCL and Lewis(x) is analogous to the way that selectins and DC-SIGN bind to related fucosylated glycans, but the mechanism of the interaction is novel, because it is based on a primary galactose-binding site similar to the binding site in the asialoglycoprotein receptor. Crystals of the human receptor lacking bound calcium ions reveal an alternative conformation in which a glycan ligand would be released during receptor-mediated endocytosis.
Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis(x) by a novel mechanism.,Feinberg H, Taylor ME, Weis WI J Biol Chem. 2007 Jun 8;282(23):17250-8. Epub 2007 Apr 9. PMID:17420244[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakamura K, Funakoshi H, Miyamoto K, Tokunaga F, Nakamura T. Molecular cloning and functional characterization of a human scavenger receptor with C-type lectin (SRCL), a novel member of a scavenger receptor family. Biochem Biophys Res Commun. 2001 Feb 2;280(4):1028-35. PMID:11162630 doi:http://dx.doi.org/10.1006/bbrc.2000.4210
- ↑ Ohtani K, Suzuki Y, Eda S, Kawai T, Kase T, Keshi H, Sakai Y, Fukuoh A, Sakamoto T, Itabe H, Suzutani T, Ogasawara M, Yoshida I, Wakamiya N. The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells. J Biol Chem. 2001 Nov 23;276(47):44222-8. Epub 2001 Sep 19. PMID:11564734 doi:http://dx.doi.org/10.1074/jbc.M103942200
- ↑ Yoshida T, Tsuruta Y, Iwasaki M, Yamane S, Ochi T, Suzuki R. SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn antigen. J Biochem. 2003 Mar;133(3):271-7. PMID:12761161
- ↑ Coombs PJ, Graham SA, Drickamer K, Taylor ME. Selective binding of the scavenger receptor C-type lectin to Lewisx trisaccharide and related glycan ligands. J Biol Chem. 2005 Jun 17;280(24):22993-9. Epub 2005 Apr 21. PMID:15845541 doi:http://dx.doi.org/M504197200
- ↑ Nakamura K, Ohya W, Funakoshi H, Sakaguchi G, Kato A, Takeda M, Kudo T, Nakamura T. Possible role of scavenger receptor SRCL in the clearance of amyloid-beta in Alzheimer's disease. J Neurosci Res. 2006 Sep;84(4):874-90. PMID:16868960 doi:http://dx.doi.org/10.1002/jnr.20992
- ↑ Feinberg H, Taylor ME, Weis WI. Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis(x) by a novel mechanism. J Biol Chem. 2007 Jun 8;282(23):17250-8. Epub 2007 Apr 9. PMID:17420244 doi:10.1074/jbc.M701624200
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