2JH1

Crystal structure of Toxoplasma gondii micronemal protein 1

2JH1 の概要

• エントリーDOI: 10.2210/pdb2jh1/pdb
• 関連するPDBエントリー: 2BVB 2JH7 2JHD
• 分子名称: MICRONEMAL PROTEIN 1, ACETATE ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: cell adhesion, mic1, microneme, mar domain, cell invasion
• 由来する生物種: TOXOPLASMA GONDII
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28312.97

構造登録者

Blumenschein, T.M.A.,Friedrich, N.,Childs, R.A.,Saouros, S.,Carpenter, E.P.,Campanero-Rhodes, M.A.,Simpson, P.,Koutroukides, T.,Blackman, M.J.,Feizi, T.,Soldati-Favre, D.,Matthews, S. (登録日: 2007-02-19, 公開日: 2007-05-22, 最終更新日: 2024-10-16)

主引用文献

Blumenschein, T.M.A.,Friedrich, N.,Childs, R.A.,Saouros, S.,Carpenter, E.P.,Campanero-Rhodes, M.A.,Simpson, P.,Chai, W.,Koutroukides, T.,Blackman, M.J.,Feizi, T.,Soldati-Favre, D.,Matthews, S.
Atomic Resolution Insight Into Host Cell Recognition by Toxoplasma Gondii.
Embo J., 26:2808-, 2007

PubMed Abstract: The obligate intracellular parasite Toxoplasma gondii, a member of the phylum Apicomplexa that includes Plasmodium spp., is one of the most widespread parasites and the causative agent of toxoplasmosis. Micronemal proteins (MICs) are released onto the parasite surface just before invasion of host cells and play important roles in host cell recognition, attachment and penetration. Here, we report the atomic structure for a key MIC, TgMIC1, and reveal a novel cell-binding motif called the microneme adhesive repeat (MAR). Using glycoarray analyses, we identified a novel interaction with sialylated oligosaccharides that resolves several prevailing misconceptions concerning TgMIC1. Structural studies of various complexes between TgMIC1 and sialylated oligosaccharides provide high-resolution insights into the recognition of sialylated oligosaccharides by a parasite surface protein. We observe that MAR domains exist in tandem repeats, which provide a highly specialized structure for glycan discrimination. Our work uncovers new features of parasite-receptor interactions at the early stages of host cell invasion, which will assist the design of new therapeutic strategies.

PubMed: 17491595
DOI: 10.1038/SJ.EMBOJ.7601704

実験手法

X-RAY DIFFRACTION (1.9 Å)