1dqo
From Proteopedia
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- | [[Image:1dqo.png|left|200px]] | ||
- | + | ==Crystal structure of the cysteine rich domain of mannose receptor complexed with Acetylgalactosamine-4-sulfate== | |
+ | <StructureSection load='1dqo' size='340' side='right'caption='[[1dqo]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1dqo]] 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=1DQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQO 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]] 2.2Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASG:2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE'>ASG</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=1dqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqo OCA], [https://pdbe.org/1dqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqo RCSB], [https://www.ebi.ac.uk/pdbsum/1dqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqo ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == 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 == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqo_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=1dqo ConSurf]. | ||
+ | <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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1dqo" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | < | + | </StructureSection> |
+ | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[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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Current revision
Crystal structure of the cysteine rich domain of mannose receptor complexed with Acetylgalactosamine-4-sulfate
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Categories: Large Structures | Mus musculus | Bjorkman PJ | Chirino AJ | Feizi T | Leteux C | Liu Y | Misulovin Z | Nussenzweig MC