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Volume 3, Issue 4, Pages 457-464 (April 1999) The Crystal Structure of C-Terminal Merozoite Surface Protein 1 at 1.8 Å Resolution, a Highly Protective Malaria Vaccine Candidate Véronique Chitarra, Inge Holm, Graham A. Bentley, Stephane Pêtres, Shirley Longacre Molecular Cell Volume 3, Issue 4, Pages 457-464 (April 1999) DOI: 10.1016/S1097-2765(00)80473-6

Figure 1 Structure of MSP1inv (A and B) Two orthogonal views of MSP1inv from P. cynomolgi showing main-chain atoms. In (A), the N and C termini are denoted by N and C, respectively. Molecular Cell 1999 3, 457-464DOI: (10.1016/S1097-2765(00)80473-6)

Figure 2 Comparison of MSP1inv Domains Stereo view of the superposition of the first domain of MSP1inv (green) onto the second domain (purple). Cystine residues are shown in yellow. Molecular Cell 1999 3, 457-464DOI: (10.1016/S1097-2765(00)80473-6)

Figure 3 Sequence Comparisons and Location of Conserved Residues of MSP1inv (A) Sequence alignment of MSP1inv from different species. Strictly conserved residues are indicated by the vertical trace, and residues making significant interdomain contacts in the crystal structure of P. cynomolgi are highlighted (bullets). N- and C-terminal residues are inferred from alignment with those determined for P. falciparum. Sequences were taken from the following sources: P. cynomolgi, Longacre 1995; P. vivax (Belem strain), del Portillo et al. 1991; P. knowlesi, Blackman et al. 1996; P. chabaudi (1), Deleersnijder et al. 1990; P. chabaudi (2), McKean et al. 1993; P. yoelii, Lewis 1989; P. berghei, Jennings et al. 1998; P. falciparum (Uganda-Palo Alto isolate), Chang et al. 1988. Underlined residues indicate experimentally determined N termini for MSP1inv. (B) Distribution of conserved residues among different species of Plasmodium; conserved cystines (yellow) and side chains of other invariant residues (red) are displayed on the polypeptide backbone (blue). (C) Residues involved in interdomain contacts. Side chains of invariant residues are shown in red, those with conservative differences are shown in green, and those with nonconservative changes are shown in purple. Molecular Cell 1999 3, 457-464DOI: (10.1016/S1097-2765(00)80473-6)

Figure 4 Location of Sequence Differences with Respect to P. cynomolgi and Polymorphic Residues in Different Species of MSP1inv Location of sequence differences with respect to P. cynomolgi and polymorphic residues in different species of MSP1inv: (A) P. falciparum and (B) P. vivax. α carbon positions are those from the crystal structure of P. cynomolgi, with the insertion 66a, 66b, 66e, and 66f introduced to give a model for P. falciparum in (A). Residues different from P. cynomolgi are shown in red (and numbered in white), and those that are also dimorphic are numbered in green. Molecular Cell 1999 3, 457-464DOI: (10.1016/S1097-2765(00)80473-6)