Liver-expressed antimicrobial peptides are a family of mammalian liver-expressed antimicrobial peptides (LEAP). The exact function of this family is unclear.
| LEAP2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | LEAP2 | ||||||||
| Pfam | PF07359 | ||||||||
| InterPro | IPR009955 | ||||||||
| OPM superfamily | 276 | ||||||||
| OPM protein | 2l1q | ||||||||
| |||||||||
LEAP2 is a cysteine-rich, and cationic protein with a core structure stabilized by two disulphide bonds formed by cysteine residues in 1-3 and 2-4 relative positions. Synthesised as a 77-residue precursor, LEAP2 is predominantly expressed in the liver and highly conserved among mammals. The largest native LEAP2 form of 40 amino acid residues is generated from the precursor at a putative cleavage site for a furin-like endoprotease. In contrast to smaller LEAP-2 variants, this peptide exhibits dose-dependent antimicrobial activity against selected microbial model organisms.[1]
References
edit- ^ Krause A, Sillard R, Kleemeier B, Klüver E, Maronde E, Conejo-GarcÃa JR, Forssmann WG, Schulz-Knappe P, Nehls MC, Wattler F, Wattler S, Adermann K (January 2003). "Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver". Protein Sci. 12 (1): 143–52. doi:10.1110/ps.0213603. PMC 2312392. PMID 12493837.