1dqg
From Proteopedia
(Difference between revisions)
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<StructureSection load='1dqg' size='340' side='right'caption='[[1dqg]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1dqg' size='340' side='right'caption='[[1dqg]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1dqg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1dqg]] is a 1 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=1DQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQG FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1dqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqg OCA], [https://pdbe.org/1dqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqg RCSB], [https://www.ebi.ac.uk/pdbsum/1dqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqg 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=1dqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqg OCA], [https://pdbe.org/1dqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqg RCSB], [https://www.ebi.ac.uk/pdbsum/1dqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/MRC1_MOUSE MRC1_MOUSE] 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. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dqg ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dqg ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The macrophage and epithelial cell mannose receptor (MR) binds carbohydrates on foreign and host molecules. Two portions of MR recognize carbohydrates: tandemly arranged C-type lectin domains facilitate carbohydrate-dependent macrophage uptake of infectious organisms, and the NH(2)-terminal cysteine-rich domain (Cys-MR) binds to sulfated glycoproteins including pituitary hormones. To elucidate the mechanism of sulfated carbohydrate recognition, we determined crystal structures of Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine at 1.7 and 2.2 A resolution, respectively. Cys-MR folds into an approximately three-fold symmetric beta-trefoil shape resembling fibroblast growth factor. The sulfate portions of 4-sulfated-N-acetylgalactosamine and an unidentified ligand found in the native crystals bind in a neutral pocket in the third lobe. We use the structures to rationalize the carbohydrate binding specificities of Cys-MR and compare the recognition properties of Cys-MR with other beta-trefoil proteins. | ||
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- | Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand.,Liu Y, Chirino AJ, Misulovin Z, Leteux C, Feizi T, Nussenzweig MC, Bjorkman PJ J Exp Med. 2000 Apr 3;191(7):1105-16. PMID:10748229<ref>PMID:10748229</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1dqg" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: Bjorkman | + | [[Category: Bjorkman PJ]] |
- | [[Category: Chirino | + | [[Category: Chirino AJ]] |
- | [[Category: Feizi | + | [[Category: Feizi T]] |
- | [[Category: Leteux | + | [[Category: Leteux C]] |
- | [[Category: Liu | + | [[Category: Liu Y]] |
- | [[Category: Misulovin | + | [[Category: Misulovin Z]] |
- | [[Category: Nussenzweig | + | [[Category: Nussenzweig MC]] |
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Revision as of 09:52, 20 March 2024
CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR
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Categories: Large Structures | Mus musculus | Bjorkman PJ | Chirino AJ | Feizi T | Leteux C | Liu Y | Misulovin Z | Nussenzweig MC