Cathelicidins are a family of antimicrobial peptides acting as multifunctional effector molecules of innate immunity, which are first found in mammals. In snake
, they show the same activity.
Most cathelicidins are linear molecules without disulfide bridges, characterized by the presence of a highly conserved anionic cathelin domain. The precursors are composed of a signal peptide, a conserved propeptide cathelin domain (about 135 residues long) and a C-terminal mature antimicrobial peptide (about 34 residues). Upon activation, most of cathelicidin precursors are proteolytically cleaved to release the cathelin domain and the C-terminal mature antimicrobial peptides (
Zhao et al., 2008
This protein family in
SIB Swiss Institute of Bioinformatics
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