Alterations in Immune-Related Defensin Alpha 4 (DEFA4) Gene Expression in Health and Disease

Figure 1

This figure shows the structure-related DEFA4 properties. Created with BioRender.com. (a) Alignments of the amino acid sequences that show conserved residues: 6 Cysteine residues (C) are shown in yellow; Glycine (G) is colored in green, Arginine (R) is located after the second Cysteine, Glutamic acid (E). Positively-charged residues are colored in blue, negatively-charged residues are colored in red. Relative to DEFA1–3 (+3), DEFA4 is the higher positive charge of (+4). This figure also shows the bonds that stabilize the α-defensins tertiary structure, 3 disulfide bridges between 6 conserved (C) and one salt bridge formed by the side chains of R and (E). (b) Three clustered cationic residues of Arginine (Arg10, Arg11, Arg15). (c) DEFA4 consists of three beta-sheets (B) arranged into an antiparallel structure. B1and B2 are connected by the long loop (T1), and beta-hairpin (T2) is formed by B2 and B3. DEFA4 forms homodimers [46].