Biology:Liver-expressed antimicrobial peptide
| LEAP2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | LEAP2 | ||||||||
| Pfam | PF07359 | ||||||||
| InterPro | IPR009955 | ||||||||
| OPM superfamily | 276 | ||||||||
| OPM protein | 2l1q | ||||||||
| |||||||||
Liver-expressed antimicrobial peptides are a family of mammalian liver-expressed antimicrobial peptides (LEAP). The exact function of this family is unclear.
LEAP2 is a cysteine-rich, and cationic protein. LEAP2 contains a core structure with two disulphide bonds formed by cysteine residues in relative 1-3 and 2-4 positions. LEAP2 is synthesised as a 77-residue precursor, which 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
- ↑ "Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver". Protein Sci. 12 (1): 143–52. January 2003. doi:10.1110/ps.0213603. PMID 12493837.
 |  |
