2ll3
From Proteopedia
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==The solution structure of TgMIC4 apple-5 domain== | ==The solution structure of TgMIC4 apple-5 domain== | ||
| - | <StructureSection load='2ll3' size='340' side='right' caption='[[2ll3 | + | <StructureSection load='2ll3' size='340' side='right'caption='[[2ll3]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2ll3]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ll3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LL3 FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=2ll3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ll3 OCA], [https://pdbe.org/2ll3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ll3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ll3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ll3 ProSAT]</span></td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[ | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MIC4_TOXGO MIC4_TOXGO] Adhesin. Required for attachment of the parasite to the host cell prior to invasion.<ref>PMID:11053441</ref> <ref>PMID:11157983</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Toxosplasma gondii is the model parasite of the phylum Apicomplexa, which contains numerous obligate intracellular parasites of medical and veterinary importance, including Eimeria, Sarcocystis, Cryptosporidium, Cyclospora and Plasmodium species. Members of this phylum actively enter host cells by a multi-step process with the help of microneme protein (MIC) complexes that play important roles in motility, host cell attachment, moving junction formation and invasion. Toxoplasma gondii (Tg)MIC1-4-6 complex is the most extensively investigated microneme complex which contributes to host cell recognition and attachment via the action of TgMIC1, a sialic acid-binding adhesin. Here, we report the structure of TgMIC4 and reveal its carbohydrate-binding specificity to a variety of galactose-containing carbohydrate ligands. The lectin is composed of six apple domains in which the fifth domain displays a potent galactose-binding activity, and which is cleaved from the complex during parasite invasion. We propose that galactose recognition by TgMIC4 masks the recognition of the parasite thereby providing protection from galectin-mediated activation of the host immune system. | Toxosplasma gondii is the model parasite of the phylum Apicomplexa, which contains numerous obligate intracellular parasites of medical and veterinary importance, including Eimeria, Sarcocystis, Cryptosporidium, Cyclospora and Plasmodium species. Members of this phylum actively enter host cells by a multi-step process with the help of microneme protein (MIC) complexes that play important roles in motility, host cell attachment, moving junction formation and invasion. Toxoplasma gondii (Tg)MIC1-4-6 complex is the most extensively investigated microneme complex which contributes to host cell recognition and attachment via the action of TgMIC1, a sialic acid-binding adhesin. Here, we report the structure of TgMIC4 and reveal its carbohydrate-binding specificity to a variety of galactose-containing carbohydrate ligands. The lectin is composed of six apple domains in which the fifth domain displays a potent galactose-binding activity, and which is cleaved from the complex during parasite invasion. We propose that galactose recognition by TgMIC4 masks the recognition of the parasite thereby providing protection from galectin-mediated activation of the host immune system. | ||
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Galactose recognition by the apicomplexan parasite Toxoplasma gondii.,Marchant J, Cowper B, Liu Y, Lai L, Pinzan C, Marq JB, Friedrich N, Sawmynaden K, Liew L, Chai W, Childs RA, Saouros S, Simpson P, Roque Barreira MC, Feizi T, Soldati-Favre D, Matthews S J Biol Chem. 2012 Mar 7. PMID:22399295<ref>PMID:22399295</ref> | Galactose recognition by the apicomplexan parasite Toxoplasma gondii.,Marchant J, Cowper B, Liu Y, Lai L, Pinzan C, Marq JB, Friedrich N, Sawmynaden K, Liew L, Chai W, Childs RA, Saouros S, Simpson P, Roque Barreira MC, Feizi T, Soldati-Favre D, Matthews S J Biol Chem. 2012 Mar 7. PMID:22399295<ref>PMID:22399295</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2ll3" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Toxoplasma gondii]] | [[Category: Toxoplasma gondii]] | ||
| - | [[Category: Cowper | + | [[Category: Cowper B]] |
| - | [[Category: Matthews | + | [[Category: Matthews S]] |
| - | + | ||
Current revision
The solution structure of TgMIC4 apple-5 domain
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