Figure 1 | Scientific Reports

Figure 1

From: The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics

Figure 1

The structure of LL-37DPC-4 provides insights into the putative transmembrane channel architecture. (A) LL-37DPC-4 in surface representation and analysis of IF1-IF3 viewing the side dominated by hydrophobic residues emphasized in green and marked by sequence numbers. The IF1 is formed by hydrophobic residues, while IF2 and IF3 are formed by a mix of polar and charged residues (marked magenta, red and blue surface). Residues involved in the maintenance of each interface are marked by numbers. (B) Aromatic girdles in the tetrameric arrangement indicate the potential for membrane integration architecture. Two phenylalanines of each peptide (Phe17 and Phe27) contribute to the formation of these regular girdles separated by a distance of ~ 1.5 nm.

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