Figure 3 | Heredity

Figure 3

From: Positive selection in cathelicidin host defense peptides: adaptation to exogenous pathogens or endogenous receptors?

Figure 3

Multiple sequence alignment of the CAP18-MP family from mammals. Cationic and anionic amino acids are shown in blue and red, respectively, and sites identified to be under positive selection are shadowed in yellow. The NMR structure of human LL-37 (Wang, 2008) is used to map PSSs and define secondary structure element regions, which comprises three distinct parts: NDR (amino-terminal disordered region, residue 1), MHR (middle α-helical region, residues 2–31) and CDR (carboxyl-terminal disordered region, residues 32–37), in which regions forming a conserved amphipathic architecture is boxed in green. NC, net charge; GRAVY, grand average of hydropathicity, which was calculated by ProtParam as the sum of hydropathy values of all the amino acids, divided by the number of residues in the sequence (http://web.expasy.org/protparam/); S(%), sequence similarity percentage.

Back to article page