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PDBsum entry 2k2s
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Cell adhesion
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PDB id
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2k2s
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References listed in PDB file
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Key reference
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Title
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Structural insights into microneme protein assembly reveal a new mode of egf domain recognition.
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Authors
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K.Sawmynaden,
S.Saouros,
N.Friedrich,
J.Marchant,
P.Simpson,
B.Bleijlevens,
M.J.Blackman,
D.Soldati-Favre,
S.Matthews.
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Ref.
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Embo Rep, 2008,
9,
1149-1155.
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PubMed id
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Abstract
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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. Adhesive complexes composed
of microneme proteins (MICs) are secreted onto the parasite surface from
intracellular stores and fulfil crucial roles in host-cell recognition,
attachment and penetration. Here, we report the high-resolution solution
structure of a complex between two crucial MICs, TgMIC6 and TgMIC1. Furthermore,
we identify two analogous interaction sites within separate epidermal growth
factor-like (EGF) domains of TgMIC6-EGF2 and EGF3-and confirm that both
interactions are functional for the recognition of host cell receptor in the
parasite, using immunofluorescence and invasion assays. The nature of this new
mode of recognition of the EGF domain and its abundance in apicomplexan surface
proteins suggest a more generalized means of constructing functional assemblies
by using EGF domains with highly specific receptor-binding properties.
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