title: The role of scaffolding in standard mechanism serine proteinase inhibitors.
abstract: In single domain, "standard mechanism" protein inhibitors of serine proteinases, about a dozen residues make contact with the cognate enzyme. The remainder of the molecule, the scaffolding, holds the reactive site region of the inhibitor in a canonical conformation, improves the binding by about six orders of magnitude and protects it from proteolysis. However, the stability and global structure of the scaffolding is irrelevant to inhibition, provided that inhibition is measured much below the melting temperature, Tm.
authors: Department of Chemistry, 560 Oval Drive, Purdue University, West Lafayette, IN 47907, USA.
authors: Clyde A
authors: CA
authors: Kelly
authors: Michael
authors: M
authors: Laskowski
authors: M A
authors: MA
authors: Qasim
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000502:physiology*; D013329:Structure-Activity Relationship; D013696:Temperature
chemical_list: D015842:Serine Proteinase Inhibitors