Article
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
Nature structural biology - 1 Feb 2000
Li M, Phylip L H, Lees W E, Winther J R, Dunn B M, Wlodawer A, Kay J, Gustchina A
Abstract excerpt
Aspartic proteinase A from yeast is specifically and potently inhibited by a small protein called IA3 from Saccharomyces cerevisiae. Although this inhibitor consists of 68 residues, we show that the inhibitory activity resides within the N-terminal half of the molecule. Structures solved at 2.2 and 1.8 A, respectively, for complexes of proteinase A with full-length IA3 and with a truncated form consisting only of...
Topics
- Amino Acid Sequence
- Aspartic Acid Endopeptidases
- Circular Dichroism
- Crystallography, X-Ray
- Fungal Proteins
- Hydrogen-Ion Concentration
- Methionine
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Folding
- Recombinant Proteins
- Saccharomyces cerevisiae