Figure 1 | Scientific Reports

Figure 1

From: A high-performance thioredoxin-based scaffold for peptide immunogen construction: proof-of-concept testing with a human papillomavirus epitope

Figure 1

Alignment of putative archaebacterial thioredoxins with E. coli, mouse and human thioredoxin.

(a) Predicted thioredoxin polypeptides from the archaebacteria M. thermophila (Acc. n. YP_843141.1) and P. furiosus (Acc. n. NP_578470.1) are aligned with homologous thioredoxins from E. coli (Acc. n. YP 003038425), M. musculus (Acc. n. NP_035790) and H. sapiens (Acc. n. AY004872) (see Supplementary Fig. S1 for an extended phylogeny of bacterial thioredoxins). Amino acids that are identical in all or in three out of the five reported sequences are shown on a black or grey background, respectively. The conserved active (display) site is boxed. (b) Predicted secondary structures of the five thioredoxin polypeptides; β sheets and α helixes are shown on a blue and a red background, respectively. The 3D structure of E. coli thioredoxin (PDB accession code: 2trx) is shown on the right with the two Cys residues of the redox active/display site represented in a ball and stick format. (c) Amino acid sequence identity values for the five thioredoxin polypeptides addressed in this study.

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