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| | <StructureSection load='4c9f' size='340' side='right'caption='[[4c9f]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='4c9f' size='340' side='right'caption='[[4c9f]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4c9f]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C9F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4c9f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GQ1:4-O-SULFO-ALPHA-D-GLUCOPYRANOSE'>GQ1</scene>, <scene name='pdbligand=GQ2:6-O-ALPHA-D-GLUCOPYRANOSYL-4-O-SULFO-ALPHA-D-GLUCOPYRANOSE'>GQ2</scene>, <scene name='pdbligand=GQ4:ALPHA-D-GLUCOPYRANOSYL-(1- 6)-ALPHA-D-GLUCOPYRANOSYL-(1- 6)-ALPHA-D-GLUCOPYRANOSYL-(1- 6)-4-O-SULFO-ALPHA-D-GLUCOPYRANOSE'>GQ4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.6Å</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=4c9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9f OCA], [http://pdbe.org/4c9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c9f RCSB], [http://www.ebi.ac.uk/pdbsum/4c9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9f ProSAT]</span></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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GQ1:4-O-SULFO-ALPHA-D-GLUCOPYRANOSE'>GQ1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4c9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9f OCA], [https://pdbe.org/4c9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9f RCSB], [https://www.ebi.ac.uk/pdbsum/4c9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/C209B_MOUSE C209B_MOUSE]] Probable pathogen-recognition receptor. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. May recognize in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. | + | [https://www.uniprot.org/uniprot/C209B_MOUSE C209B_MOUSE] Probable pathogen-recognition receptor. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. May recognize in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Anthony, R M]] | + | [[Category: Anthony RM]] |
| - | [[Category: Bartual, S G]] | + | [[Category: Bartual SG]] |
| - | [[Category: Chacon, P]] | + | [[Category: Chacon P]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Hermoso JA]] |
| - | [[Category: Park, C G]] | + | [[Category: Park CG]] |
| - | [[Category: Ramirez, E]] | + | [[Category: Ramirez E]] |
| - | [[Category: Rodriguez, A]] | + | [[Category: Rodriguez A]] |
| - | [[Category: Silva-Martin, N]] | + | [[Category: Silva-Martin N]] |
| - | [[Category: C-type lectin]]
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| - | [[Category: Innate immunity]]
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| - | [[Category: Membrane protein]]
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| Structural highlights
Function
C209B_MOUSE Probable pathogen-recognition receptor. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. May recognize in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates.
Publication Abstract from PubMed
SIGN-R1 is a principal receptor for microbial polysaccharides uptake and is responsible for C3 fixation via an unusual complement activation pathway on splenic marginal zone macrophages. In these macrophages, SIGN-R1 is also involved in anti-inflammatory activity of intravenous immunoglobulin by direct interaction with sialylated Fcs. The high-resolution crystal structures of SIGN-R1 carbohydrate recognition domain and its complexes with dextran sulfate or sialic acid, and of the sialylated Fc antibody provide insights into SIGN-R1's selective recognition of a-2,6-sialylated glycoproteins. Unexpectedly, an additional binding site has been found in the SIGNR1 carbohydrate recognition domain, structurally separate from the calcium-dependent carbohydrate-binding site. This secondary binding site could bind repetitive molecular patterns, as observed in microbial polysaccharides, in a calcium-independent manner. These two binding sites may allow SIGNR1 to simultaneously bind both immune glycoproteins and microbial polysaccharide components, accommodating SIGN-R1's ability to relate the recognition of microbes to the activation of the classical complement pathway.
Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1.,Silva-Martin N, Bartual SG, Ramirez-Aportela E, Chacon P, Park CG, Hermoso JA Structure. 2014 Nov 4;22(11):1595-606. PMID:25450767[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Silva-Martin N, Bartual SG, Ramirez-Aportela E, Chacon P, Park CG, Hermoso JA. Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1. Structure. 2014 Nov 4;22(11):1595-606. PMID:25450767 doi:http://dx.doi.org/10.1016/j.str.2014.09.001
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