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. Author manuscript; available in PMC: 2008 Dec 24.

Published in final edited form as: FEBS Lett. 2008 Jan 15;582(4):485–490. doi: 10.1016/j.febslet.2008.01.008

Fig. 1 — Chagasin residues targeted for mutagenesis. A Sequence alignment of chagasin (AJ299433), L. major ICP (AJ548878), L. mexicana ICP (AJ548776) and T. brucei ICP (AJ548777). The secondary structure is assigned on top and the conserved motifs are marked in bold. Conserved residues in loops L2, L4 and L6 are coloured blue, magenta, and green. The residues selected for site-directed mutagenesis are underlined. B Detail of the modeled interface between chagasin (beige) and cruzain (grey). Chagasin loops L2, L4 and L6 are coloured blue, magenta and green respectively. Residues responsible for direct peptidase recognition and the peptidase’s catalytic triad are shown as sticks, and those mutated in this study are labeled and highlighted as fatter sticks.

Fig. 1 — Chagasin residues targeted for mutagenesis. A Sequence alignment of chagasin (AJ299433), L. major ICP (AJ548878), L. mexicana ICP (AJ548776) and T. brucei ICP (AJ548777). The secondary structure is assigned on top and the conserved motifs are marked in bold. Conserved residues in loops L2, L4 and L6 are coloured blue, magenta, and green. The residues selected for site-directed mutagenesis are underlined. B Detail of the modeled interface between chagasin (beige) and cruzain (grey). Chagasin loops L2, L4 and L6 are coloured blue, magenta and green respectively. Residues responsible for direct peptidase recognition and the peptidase’s catalytic triad are shown as sticks, and those mutated in this study are labeled and highlighted as fatter sticks.