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. 2012 Dec 11;109(52):21420–21425. doi: 10.1073/pnas.1218581109

Fig. 1.

Fig. 1.

Structure of TRAP. (A) Domain organization, to scale by sequence position. Structure of P. falciparum 41-240 fragment (B, closed) and P. vivax 25-283 fragment (C, open) shown in identical orientations. Domains are colored (B and C) according to the key in (A), whereas the VWA β6-α7 loop and α7-helix are white. Disulfide bonds (yellow) and O-linked glycans are shown as sticks. Details near the extensible β ribbon in the closed conformation in P. falciparum 26-299 (D), P. falciparum 41-240 (E), and P. vivax (F) are shown in identical orientations. Sidechains are shown in stick. (G) Sequence alignment of P. vivax and P. falciparum TRAP, with secondary structures in the open and closed conformations shown above and below the alignment, respectively. Disordered residues are italicized. MIDAS residues are asterisked. Dots mark decadal residues.