Liver-expressed antimicrobial peptide

Liver-expressed antimicrobial peptides are a family of mammalian liver-expressed antimicrobial peptides (LEAP). The exact function of this family is unclear.

LEAP2
Identifiers
SymbolLEAP2
PfamPF07359
InterProIPR009955
OPM superfamily276
OPM protein2l1q
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

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  1. ^ 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.
This article incorporates text from the public domain Pfam and InterPro: IPR009955