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Results: 2

Figure 1

Figure 1. From: Receptor-ligand interaction and invasion: Microneme proteins in apicomplexans.

Modular MICs.
Schematic representations of known microneme proteins from four different apicomplexan genera are depicted (not to scale). Accession numbers, where available: Eimeria tenella MIC1, M73495; EtMIC2, Z71755; EtMIC3, AAR87667; EtMIC4, CAC34726; EtMIC5, AJ245536; Cryptosporidium parvum TRAP-C1, AAB92609; GP900, AAC98153; CpSCRP AF061328; Plasmodium falciparum TRAP, AAC1867; Plasmodium berghei SPECT, BAD08209; PbSPECT2, BAD83404; PbCelTOS, BAD97683; PbSOAP, AAL07530; PbCHT1, CAC40151; PbWARP, AAK83296; PbMOAP, AAV28504; PbCTRP, AAF73158; Toxoplasma gondii MIC1, CAA96466; TgMIC2, AAB63303; TgM2AP, AAK74070; TgMIC3, CAB56644; TgMIC4 AAD33906; TgMIC5, CAA70921; TgMIC6, AAD28185; TgMIC7, AAK35070; TgMIC8, AAK19757; TgMIC9, AAK19758; TgMIC10, AAG32024; TgMIC11, AAN16379; TgMIC12, AAK58479; TgAMA1, AF010264; TgSUB1, AAK94670.

Vern B. Carruthers, et al. Subcell Biochem. ;47:33-45.
Figure 2

Figure 2. From: Receptor-ligand interaction and invasion: Microneme proteins in apicomplexans.

Structural features of micronemal ligands.
(A) MICs from Eimeria (EtMIC4-MIC5), Toxoplasma (TgMIC1-4-6, TgMIC2-M2AP) and Plasmodium (PvAMA1) are schematically depicted with a scale (left) illustrating the approximate distance they would project from the parasite membrane, assuming a fully elongated state. Projection estimates are based on the dimensions of the domain types shown as ribbon structures, with α-helices (red), β-sheets (blue), and random coils or turns (grey). Structures are based on the following: cbEGF from fibrillin (Protein Data Bank accession number 1EMO), PAN/Apple from EtMIC5 (1HKY), A/I domain from integrin αL (1MQA), TSR from thrombospondin (1LSL), ectodomain of PvAMA1 (1W8K). (B) Model based on80 of an integrin heterodimer in the closed (low affinity) and the open (high affinity) configuration.

Vern B. Carruthers, et al. Subcell Biochem. ;47:33-45.

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