4c9f: Difference between revisions

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 <StructureSection load='4c9f' size='340' side='right'caption='[[4c9f]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == 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='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'>[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='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>
 == 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;">
-== 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<ref>PMID:25450767</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4c9f" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
 [[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]]
-[[Category: Innate immunity]]
-[[Category: Membrane protein]]