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. 2020 Mar 20;10:5088. doi: 10.1038/s41598-020-61714-8

Figure 3.

Figure 3

Tertiary structures of PZP and A2ML1. The structure of human PZP was predicted based on published amino acid sequences (NP_002855.2 and P20742) (A). A2M_N: Macroglobulin domain of alpha-2-macroglobulin; A2M_N_2: Alpha-2-macroglobulin family N-terminal region; A2M: Alpha-2-macroglobulin family C-terminal region; A2M_comp: A-macroglobulin complement component; A2M_recep: A-macroglobulin receptor; BAIT region: protease binding regions; Thiol-ester site: sequence that shows conformational change after protease binding; S-S: disulfide moiety; boxed numerals (1–36): exon number; 400-800-1200-1400: amino acid location. I: Amino acid sequence upstream of bait region; II: amino acid sequence of bait region; III: amino acid sequence downstream of C-terminal region after the bait region. Panels B–F: Predicted tertiary structures of human PZP dimer (B), human PZP monomer (C), human A2ML1 monomer (D), marmoset PZP monomer (E), and marmoset A2ML1 monomer (F). Different areas are represented by the following colours: Bait region, white; Proline-endopeptidase cutting site, pink; Aspartic acid-N endopeptidase cutting site, black; LysC, orange; LysN, yellow.