title: Structure-activity relationship within the serine protease inhibitors of the pacifastin family.
abstract: The members of the Pacifastin family are serine protease inhibitors found in insects and crustacean. They are either small inhibitors (made of one consensus cysteine-rich motif) or proteins (4-9 motifs). Some of these inhibitors are characterized by a species selectivity for the trypsin inhibition. Structural data discriminate the small inhibitors that apparently look very similar into two groups. Interestingly, the inhibitors that display species selectivity fall in the same structural group.
authors: Centre d'Immunologie de Marseille-Luminy, UMR 145, Parc Scientifique et Technologique de Luminy - Case 906, 13288 Marseille Cedex, France. kellenberger@ciml.univ-mrs.fr
authors: Christine
authors: C
authors: Kellenberger
authors: Alain
authors: A
authors: Roussel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003445:Crustacea / Q000201:enzymology; D007313:Insecta / Q000201:enzymology; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D011506:Proteins; D015842:Serine Proteinase Inhibitors; C106709:pacifastin