Biology:LGMN

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A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Legumain is a protein that in humans is encoded by the LGMN gene.[1][2][3]

This gene encodes a cysteine protease, legumain, that has a strict specificity for hydrolysis of asparaginyl bonds. This enzyme may be involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Enzyme activation is triggered by acidic pH and appears to be autocatalytic. Protein expression occurs after monocytes differentiate into dendritic cells. A fully mature, active enzyme is produced following lipopolysaccharide expression in mature dendritic cells. Overexpression of this gene may be associated with the majority of solid tumor types. This gene has a pseudogene on chromosome 13. Several alternatively spliced transcript variants have been described, but the biological validity of only two has been determined. These two variants encode the same isoform.[3]

References

  1. "Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and its chromosome assignment to 14q32.1". Cytogenet Cell Genet 74 (1–2): 120–3. Dec 1996. doi:10.1159/000134397. PMID 8893817. 
  2. "Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase". J Biol Chem 272 (12): 8090–8. Apr 1997. doi:10.1074/jbc.272.12.8090. PMID 9065484. 
  3. 3.0 3.1 "Entrez Gene: LGMN legumain". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5641. 

Further reading