2ll4
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
[[2ll4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LL4 OCA]. <br> | [[2ll4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LL4 OCA]. <br> | ||
| - | <b>Related:</b> [[2ll3|2ll3]]<br> | + | <b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br> |
| + | <b>[[Related_structure|Related:]]</b> [[2ll3|2ll3]]<br> | ||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | ||
| + | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ll4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ll4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ll4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ll4 PDBsum]</span><br> | ||
== 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. | ||
Revision as of 10:25, 30 April 2014
HADDOCK structure of TgMIC4-A5/lacto-N-biose complex, based on NOE-derived distance restraints
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