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![[Figure 1]](ol5291fig1mag.jpg)
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Figure 1
Amino-acid sequence alignment of conkunitizin-S1 and other Kunitz proteins and domains. Highly conserved positions are shaded. Disulfide connections are shown with either a solid line or, in the case of the CysII–CysIV disulfide, a broken line. Conkunitzin-S1, the focus of this work, is a two-disulfide Kunitz-fold conotoxin isolated from C. striatus venom. Two-disulfide variants selected for comparison are cow TK-3 (amino acids 122–172 of trophoblast Kunitz domain protein-3 from cow) and Ixolaris (amino acids 101–151 of a tissue-factor pathway inhibitor from the tick Ixodes scapularis). Selected Kunitz folds with three disulfides that were superimposed to make the ensemble search model are as follows: α-dendrotoxin (a K+-channel-blocking toxin from the green mamba Dendroaspis angusticeps), collagen type VI (the C5 domain of human type VI collagen α-3 chain), TFPI-2 (amino acids 121–178 of the human tissue-factor pathway inhibitor) and BPTI (bovine pancreatic trypsin inhibitor, the first described Kunitz protein; Kunitz & Northrop, 1936  ). |
![[Figure 1]](ol5291fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
