Figure 1

The knottin fold. (Top) Stereoscopic view of a schematic representation of MCoTI-II, a head-to-tail cyclized squash inhibitor. The head-to-tail linker is shown in blue. Disulfide bridges are shown as ball-and-stick representations. The cystine knot is shown in green (the disulfide macrocycle) and orange (the penetrating disulfide). β-strands are shown as flat arrows and the 3₁₀-helix turn is shown in magenta. Cysteines are numbered. (Bottom) Sequences of the squash inhibitors used in this work. Numbering follows MCoTI-II. The disulfide bridge coloring scheme follows the one used in the structure. The colors used in the three-dimensional structure are shown using a colored line below the MCoTI-II sequence. Peptide cyclization is displayed as a black line for MCoTI-II.