View source for 5xts


==Crystal structure of the CysR-CTLD3 fragment of human MR at basic/neutral pH==
<StructureSection load='5xts' size='340' side='right'caption='[[5xts]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xts]] is a 1 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=5XTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XTS FirstGlance]. <br>
</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&#8491;</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></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=5xts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xts OCA], [https://pdbe.org/5xts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xts RCSB], [https://www.ebi.ac.uk/pdbsum/5xts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xts ProSAT]</span></td></tr>
</table>
== Function ==
[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.
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== 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<ref>PMID:29225077</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5xts" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: He Y]]
[[Category: Hu Z]]