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4A5V

Solution structure ensemble of the two N-terminal apple domains (residues 58-231) of Toxoplasma gondii microneme protein 4

4A5V の概要
エントリーDOI10.2210/pdb4a5v/pdb
NMR情報BMRB: 18039
分子名称MICRONEMAL PROTEIN 4 (1 entity in total)
機能のキーワードadhesion
由来する生物種TOXOPLASMA GONDII
細胞内の位置Cytoplasmic vesicle, secretory vesicle, microneme: Q9XZH7
タンパク質・核酸の鎖数1
化学式量合計17243.07
構造登録者
主引用文献Marchant, J.,Cowper, B.,Liu, Y.,Lai, L.,Pinzan, C.,Marq, J.B.,Friedrich, N.,Sawmynaden, K.,Liew, L.,Chai, W.,Childs, R.A.,Saouros, S.,Simpson, P.,Roque Barreira, M.C.,Feizi, T.,Soldati-Favre, D.,Matthews, S.
Galactose Recognition by the Apicomplexan Parasite Toxoplasma Gondii.
J.Biol.Chem., 287:16720-, 2012
Cited by
PubMed Abstract: 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 multistep process with the help of microneme protein (MIC) complexes that play important roles in motility, host cell attachment, moving junction formation, and invasion. T. 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 may compromise host protection from galectin-mediated activation of the host immune system.
PubMed: 22399295
DOI: 10.1074/JBC.M111.325928
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 4a5v
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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