Article
Site-specific mutagenesis reveals differences in the structural bases for tight binding of RNase inhibitor to angiogenin and RNase A.
Proceedings of the National Academy of Sciences of the United States of America - 4 Mar 1997
Chen C Z, Shapiro R
Abstract excerpt
RNase inhibitor (RI) binds with extraordinary affinity (Ki approximately 10(-13)-10(-16) M) to diverse proteins in the pancreatic RNase superfamily. In the present study, the structural basis for the recognition of two RI ligands, human angiogenin (Ang) and bovine RNase A, has been investigated b...
Topics
- Animals
- Cattle
- Enzyme Inhibitors
- Escherichia coli
- Gene Expression
- Humans
- Kinetics
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Pancreas
- Placental Hormones
- Protein Binding
- Protein Structure, Tertiary
- Proteins
- Ribonuclease, Pancreatic