Article
Mutation of a conserved amino acid residue (tryptophan 1173) in the tyrosine kinase domain of the IGF-I receptor abolishes autophosphorylation but does not eliminate biologic function.
The Journal of biological chemistry - 10 Feb 1995
Blakesley V A, Kato H, Roberts C T, LeRoith D
Abstract excerpt
The amino acid sequence of the tyrosine kinase domain of the insulin-like growth factor-I (IGF-I) receptor is 84% identical to the sequence of the analogous region of the insulin receptor. A naturally occurring mutation of the tryptophan residue at position 1200 of the insulin receptor to serine...
Topics
- 3T3 Cells
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Conserved Sequence
- DNA Primers
- Deoxyglucose
- Mice
- Molecular Sequence Data
- Mutation
- Phosphorylation
- Protein-Tyrosine Kinases
- Receptors, Somatomedin
- Signal Transduction
- Thymidine
- Tryptophan
- Tyrosine