Article
The roles of tyrosines 24, 31, and 60 in the high affinity binding of insulin-like growth factor-I to the type 1 insulin-like growth factor receptor.
The Journal of biological chemistry - 15 Sept 1990
Bayne M L, Applebaum J, Chicchi G G, Miller R E, Cascieri M A
Abstract excerpt
A series of insulin-like growth factor I (IGF-I) structural analogs in which one or more of the three tyrosine residues were replaced with nonaromatic residues were produced and their binding properties characterized. The single point mutations, [Leu24]IGF-I, [Ala31]IGF-I, and [Leu60]IGF-I result...
Topics
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- DNA
- Humans
- Insulin-Like Growth Factor I
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes
- Plasmids
- Protein Conformation
- Receptors, Cell Surface
- Receptors, Somatomedin
- Somatomedins
- Tyrosine