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. 2008 Sep 26;9(11):1149–1155. doi: 10.1038/embor.2008.179

Figure 1.

Figure 1

TgMIC6-EGF2 interacts independently with TgMIC1-GLD. (A) Schematic representation of the domain structure of TgMIC6 (top) and TgMIC1 (bottom). Microneme adhesive repeat (MAR) domain, galectin-like domain (GLD), epidermal growth factor-like (EGF), transmembrane (TM) and acidic domains are shown. The first EGF domain is proteolytically removed during transport to the micronemes. (B) Gel filtration profiles for TgMIC6-EGF2 (green), TgMIC1-GLD (orange) and TgMIC1-GLD–TgMIC6-EGF2 complex (blue). (C) Isothermal titrations of TgMIC1-GLD with TgMIC6-EGF2. Analysis of the titration data shows Kd=53±13 nM; ΔH=−1820±19 cal mol−1 and ΔS=27.2 eu. MIC, microneme proteins.