Figure 2
Structural characterization of human SERPINB5.
(a) The selected variant regions between rs2289519 and rs2289520 of five maspin-like proteins including human (NP_002630.2), mouse (NP_033283.1), rat (NP_476449.1), chicken (XP_418986.3) and frog (NP_001011282.1) using a truncated multiple sequence format. The secondary structure of SERPINB5 is shown above the alignment and the numbering is based on the human SERPINB5. Arrows represent β-strands and cylinders indicates α-helices. (b) Schematic representation of the overall human SERPINB5 protein. Domain symbols are drawn approximately to scale. The rectangles represent the key secondary structures [s2C (yellow) and s3C (pink)] that provided stabilizing interactions with the RCL (green). The positions of rs2289519, rs2289520 and rs1455555 are indicated by asterisks. (c) Ribbon diagram (ViewerLite 5.0) showing he 3D structure of human SERPINB5 (PDB accession number: 1XQG). The N-terminal and C-terminal ends are indicated with N’ and C’, respectively. The purple sphere indicated the Cα carbon of the germline variants characterized in this study. (d) Protein stability estimation of SERPINB5 SNP haplotype variation using a structure-based approach. The free energy of the protein is a weighted sum of the van der Waals, solvation, hydrogen bonding and backbone-dependent statistical energies.
