Article
Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions.
Biochemistry - 18 Feb 1992
Shoelson S E, Lu Z X, Parlautan L, Lynch C S, Weiss M A
Abstract excerpt
Mutagenesis of the dimer- and hexamer-forming surfaces of insulin yields analogues with reduced tendencies to aggregate and dramatically altered pharmacokinetic properties. We recently showed that one such analogue, HisB10----Asp, ProB28----Lys, LysB29----Pro human insulin (DKP-insulin), has enha...
Topics
- Amino Acid Sequence
- Binding Sites
- Circular Dichroism
- Humans
- Insulin
- Macromolecular Substances
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Phenylalanine
- Receptor, Insulin
- Structure-Activity Relationship