1egg

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[[Image:1egg.jpg|left|200px]]<br /><applet load="1egg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1egg, resolution 2.30&Aring;" />
 
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'''STRUCTURE OF A C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD-4) FROM THE MACROPHAGE MANNOSE RECEPTOR'''<br />
 
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==Overview==
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==STRUCTURE OF A C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD-4) FROM THE MACROPHAGE MANNOSE RECEPTOR==
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<StructureSection load='1egg' size='340' side='right'caption='[[1egg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1egg]] is a 2 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=1EGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1egg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egg OCA], [https://pdbe.org/1egg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egg RCSB], [https://www.ebi.ac.uk/pdbsum/1egg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1egg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1egg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The mannose receptor of macrophages and liver endothelium mediates clearance of pathogenic organisms and potentially harmful glycoconjugates. The extracellular portion of the receptor includes eight C-type carbohydrate recognition domains (CRDs), of which one, CRD-4, shows detectable binding to monosaccharide ligands. We have determined the crystal structure of CRD-4. Although the basic C-type lectin fold is preserved, a loop extends away from the core of the domain to form a domain-swapped dimer in the crystal. Of the two Ca(2+) sites, only the principal site known to mediate carbohydrate binding in other C-type lectins is occupied. This site is altered in a way that makes sugar binding impossible in the mode observed in other C-type lectins. The structure is likely to represent an endosomal form of the domain formed when Ca(2+) is lost from the auxiliary calcium site. The structure suggests a mechanism for endosomal ligand release in which the auxiliary calcium site serves as a pH sensor. Acid pH-induced removal of this Ca(2+) results in conformational rearrangements of the receptor, rendering it unable to bind carbohydrate ligands.
The mannose receptor of macrophages and liver endothelium mediates clearance of pathogenic organisms and potentially harmful glycoconjugates. The extracellular portion of the receptor includes eight C-type carbohydrate recognition domains (CRDs), of which one, CRD-4, shows detectable binding to monosaccharide ligands. We have determined the crystal structure of CRD-4. Although the basic C-type lectin fold is preserved, a loop extends away from the core of the domain to form a domain-swapped dimer in the crystal. Of the two Ca(2+) sites, only the principal site known to mediate carbohydrate binding in other C-type lectins is occupied. This site is altered in a way that makes sugar binding impossible in the mode observed in other C-type lectins. The structure is likely to represent an endosomal form of the domain formed when Ca(2+) is lost from the auxiliary calcium site. The structure suggests a mechanism for endosomal ligand release in which the auxiliary calcium site serves as a pH sensor. Acid pH-induced removal of this Ca(2+) results in conformational rearrangements of the receptor, rendering it unable to bind carbohydrate ligands.
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==About this Structure==
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Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor.,Feinberg H, Park-Snyder S, Kolatkar AR, Heise CT, Taylor ME, Weis WI J Biol Chem. 2000 Jul 14;275(28):21539-48. PMID:10779515<ref>PMID:10779515</ref>
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1EGG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGG OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor., Feinberg H, Park-Snyder S, Kolatkar AR, Heise CT, Taylor ME, Weis WI, J Biol Chem. 2000 Jul 14;275(28):21539-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10779515 10779515]
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</div>
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<div class="pdbe-citations 1egg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Feinberg, H.]]
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[[Category: Feinberg H]]
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[[Category: Heise, C T.]]
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[[Category: Heise CT]]
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[[Category: Kolatkar, A R.]]
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[[Category: Kolatkar AR]]
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[[Category: Park-Snyder, S.]]
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[[Category: Park-Snyder S]]
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[[Category: Taylor, M E.]]
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[[Category: Taylor ME]]
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[[Category: Weis, W I.]]
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[[Category: Weis WI]]
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[[Category: CA]]
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[[Category: c-type lectin]]
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[[Category: mannose receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:28 2008''
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Current revision

STRUCTURE OF A C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD-4) FROM THE MACROPHAGE MANNOSE RECEPTOR

PDB ID 1egg

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