Figure 2

Three-finger toxins in A. labialis venom gland. A) Alignment of long-chain neurotoxins with α-cobratoxin (α-cobra) [64]. The changed in amino acids are highlighted in grey which is either due to addition or deletion of nucleotide. ◆, conserved Cysteine residues; *, residues involved in binding to nicotinic acetylcholine receptor (nAChR); and □, residues Ala28 and Lys49 involved in binding to α7 receptor and nAChR receptor, respectively. Residues that are different from consensus sequence of A. lablialis toxins are highlighted. The truncated transcripts and the elongated protein product (clone 112; for brevity, functionally unimportant parts of the sequence are not shown and the dots indicate the missing segments). The number of clones is shown in italics and the predicted signal peptide using SignalP 3.0 is underlined (The signal peptide for α-cobrotoxin is not available). B) Alignment of two cDNA-deduced peptide representatives of one cluster and one singleton of putative short-chain neurotoxin with Erabutoxin a (Erabtx_a) [65]. The gaps in clone 6A and 12B are represented by blank spaces. *, residues involved in binding to nicotinic acetylcholine receptor (nAChR). The substitution of Thr to Ala in clone 12B is highlighted. Phe32 (□) of erabutoxin a involved in binding to nAChR receptor which is substituted with His32 in both the clones of A. labialis is highlighted. The number of clones is shown in italics and the predicted signal peptide using SignalP 3.0 is underlined.