Interaction of EGLIN C variants with the extended subsites of the precursor processing proteases.
Potent inhibitors of the Kex2/furin family precursor processing proteases were developed by randomizing adventitious contact sites and screening for optimized affinity using inhibition assays in 96-well format [1]. In this review, the binding interactions of the developed inhibitors will be examined in light of the three dimensional structures of Kex2 and furin [2-4].
Komiyama
Tomoko
T
University of Michigan Medical School, Department of Biological Chemistry, Ann Arbor, MI 48109, USA. tomokomi@umich.edu
D000595:Amino Acid Sequence; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000494:pharmacology; D045683:Furin / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry / Q000378:metabolism; D043484:Proprotein Convertases / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D015843:Serpins / Q000737:chemistry / Q000378:metabolism*
D004791:Enzyme Inhibitors; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; D015843:Serpins; C028656:eglin proteinase inhibitors; D010447:Peptide Hydrolases; D043484:Proprotein Convertases; C058751:KEX2 protein, S cerevisiae; D045683:Furin