Fig. 1

Names, cysteine patterns, and structures of representative CS-αβ peptides. a Names of representative sequences with accession numbers and alignment of mature peptide to reference array. Cysteines 3, 4, 8, and 9 form the cysteine-stabilized helix (CSH) motif, and cysteines 2 and 6 form a third bond to complete the CS-αβ fold. Alignment of all retrieved sequences to the reference array can be found in Additional file 1: Figure S1. b–m Structures of representative peptides with disulfide bonds shown in bright pink: b Sarcophaga peregrina Sapecin A [PDB: 1L4V], c Leiurus quinquestriatus hebraeus Charybdotoxin [PDB: 2CRD], d Drosophila melanogaster Drosomycin [PDB: 1MYN], e Raphanus sativus RsAFP1 [PDB: 1AYJ], f Centruroides sculpturatus CsEv2 [PDB: 1JZB], g Pseudoplectania nigrella Plectasin [PDB: 1ZFU], h Mytilus galloprovincialis MGD1 [PDB: 1FJN], i Mytilus edulis Mytilin B [PDB: 2EEM], j Ascaris suum ASABF [PDB: 2D56], k Scorpio maurus Maurotoxin [PDB: 1TXM], l Hydra magnipapillata Hydramacin [PDB: 2K35], and m Hirudo medicinalis Theromacin [PDB: 2LN8]. Major taxonomic groups are color-coded: Annelida (dark rose), Arachnida (light orange), Bivalvia (light blue), Cnidaria (light grey), Fungi (light green), Hexapoda (orange), Nematoda (lavender), Plantae (green), and Porifera (dark grey)