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| | ==Crystal structure of the CysR-CTLD2 fragment of human MR at acidic pH== | | ==Crystal structure of the CysR-CTLD2 fragment of human MR at acidic pH== |
| - | <StructureSection load='5xtw' size='340' side='right' caption='[[5xtw]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='5xtw' size='340' side='right'caption='[[5xtw]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xtw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xtw]] is a 8 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=5XTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XTW 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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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]] 3.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MRC1, CLEC13D, CLEC13DL, MRC1L1 ([http://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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=5xtw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtw OCA], [http://pdbe.org/5xtw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xtw RCSB], [http://www.ebi.ac.uk/pdbsum/5xtw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtw 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=5xtw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtw OCA], [https://pdbe.org/5xtw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xtw RCSB], [https://www.ebi.ac.uk/pdbsum/5xtw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MRC1_HUMAN MRC1_HUMAN]] Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria, fungi and other pathogens. | + | [https://www.uniprot.org/uniprot/MRC1_HUMAN MRC1_HUMAN] Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria, fungi and other pathogens. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: He, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Hu, Z]] | + | [[Category: He Y]] |
| - | [[Category: Collagen binding]] | + | [[Category: Hu Z]] |
| - | [[Category: Endocytic receptor]]
| + | |
| - | [[Category: Immune receptor]]
| + | |
| - | [[Category: Lectin-activity]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
MRC1_HUMAN Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria, fungi and other pathogens.
Publication Abstract from PubMed
Mannose receptor (MR, CD206) is an endocytic receptor on microphages and dendritic cells. It recognizes multiple ligands and plays important roles in regulating immune responses and maintaining glycoprotein homeostasis. However, the structure and functional mechanism of MR remain unclear. Here we determine the crystal structures of the N-terminal fragments of MR and reveal the potential binding mode of collagen on the fibronectin II domain. The SAXS and other biophysical data suggest that MR adopts an extended conformation at physiological pH and undergoes conformational changes as pH decreases, resulting in a compact conformation in an acidic environment. Moreover, biochemical data show that MR binds to collagen in a Ca(2+)-enhanced manner at physiological pH, whereas Ca(2+) has no effect on the binding at acidic pH. These results provide a model for the dynamic mechanism of MR regarding its ligand binding and release during the recycling between cell surface and endosomes.
Structural Insights into the pH-Dependent Conformational Change and Collagen Recognition of the Human Mannose Receptor.,Hu Z, Shi X, Yu B, Li N, Huang Y, He Y Structure. 2017 Dec 6. pii: S0969-2126(17)30359-3. doi:, 10.1016/j.str.2017.11.006. PMID:29225077[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hu Z, Shi X, Yu B, Li N, Huang Y, He Y. Structural Insights into the pH-Dependent Conformational Change and Collagen Recognition of the Human Mannose Receptor. Structure. 2017 Dec 6. pii: S0969-2126(17)30359-3. doi:, 10.1016/j.str.2017.11.006. PMID:29225077 doi:http://dx.doi.org/10.1016/j.str.2017.11.006
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