title: Selective inhibitors of human neutrophil proteinase 3.
abstract: Human neutrophil proteinase 3 (PR3) and elastase (HNE) are homologous serine proteinases involved in the proteolytic events associated with inflammation and infection. Their close structural and functional resemblance makes it difficult to understand their respective biological functions. Thus, all natural inhibitors of PR3 identified to date preferentially target HNE, and only recently have inhibitors that target PR3 selectively been described. This review describes how differences in the structures of the extended active sites of PR3 and HNE can be exploited to produce selective inhibitors of PR3.
authors.affiliation: INSERM U-1100/EA-6305 Centre d'Etudes des Pathologies Respiratoires, Université François Rabelais, Faculté de Médecine, 37032, Tours, France. brice.korkmaz@inserm.fr
authors.forename: Brice
authors.initials: B
authors.lastname: Korkmaz
authors.forename: Christine
authors.initials: C
authors.lastname: Kellenberger
authors.forename: Marie-Claude
authors.initials: MC
authors.lastname: Viaud-Massuard
authors.forename: Francis
authors.initials: F
authors.lastname: Gauthier
mesh_terms: D006801:Humans; D053146:Myeloblastin / Q000037:antagonists & inhibitors*; D011480:Protease Inhibitors / Q000494:pharmacology*; D059748:Proteolysis / Q000187:drug effects*
chemical_list: D011480:Protease Inhibitors; D053146:Myeloblastin