Article
Human epidermal growth factor. Distinct roles of tyrosine 37 and arginine 41 in receptor binding as determined by site-directed mutagenesis and nuclear magnetic resonance spectroscopy.
FEBS letters - 1 Oct 1990
Engler D A, Montelione G T, Niyogi S K
Abstract excerpt
Site-directed mutagenesis was employed to examine the function of two highly conserved residues, Tyr-37 and Arg-41, of human EGF (hEGF) in receptor binding. Both a conservative change to phenylalanine and a semi-conservative change to histidine at position 37 yield proteins with receptor affinity similar to wild-type hEGF. A non-conservative change to alanine results in a molecule with about 40% of the receptor...
Topics
- Amino Acid Sequence
- Arginine
- Binding, Competitive
- Epidermal Growth Factor
- Humans
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Receptors, Amino Acid