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. Author manuscript; available in PMC: 2009 Oct 21.
Published in final edited form as: Trends Immunol. 2009 Feb 13;30(3):131–141. doi: 10.1016/j.it.2008.12.003

Figure 1.

Figure 1

Structure of selected antimicrobial peptides (AMPs). AMPs are present in a wide variety of structural conformation, such as peptides with α-helix structures, peptides with β-sheet structures stabilized by disulfide bridges or peptides with extended or loop structures. (a) α-helix. NMR-structure of the LL-37 core peptide of cathelicidin bound to detergent micelles [PDB ID: 2FBS). (b) β-sheet Solution structure of the defensin hBD2 by two-dimensional proton nuclear magnetic resonance spectroscopy (PDB ID: 1FQQ). (c) extended structure, NMR structure of the bovine antimicrobial peptide indolicidin bound to dedecytphosphocholine (OPC) micelles (PDB ID: 1G89). (d) loop structure. 3D structure of a cyclic defensin from the leukocytes of rhesus macaques (PDB ID: 1HVZ). PDB ID: ID of peptide structure in Research Collaboratory for Structural Bioinformatics (RCSB) protein data bank (http://www.rcsb.org/pdb/home/home.do). The style of LL37 in (a) is shown as secondary coloring shortcuts, whereas the styles of peptides in (b-d) are shown in rainbow coloring shortcuts.