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FEBS Lett. 1990 Oct 1;271(1-2):47-50.

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.

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1
Protein Engineering and Molecular Mutagenesis Program, Oak Ridge National Laboratory, Tennessee 37831-8077.

Erratum in

  • FEBS Lett 1990 Oct 29;273(1-2):261.

Abstract

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 affinity, indicating that an aromatic residue is not essential at this position. Both conservative (to lysine) and non-conservative (to alanine) substitutions at position 41 drastically reduced receptor binding to less than 0.5% of the wild-type activity. 1D-NMR data indicate that the replacement of Arg-41 by lysine does not significantly alter the native protein conformation. Thus, Arg-41 may be directly involved in ligand receptor interaction, whereas the side chain of Tyr-37, although possibly important structurally, is not essential for receptor binding.

PMID:
2172006
DOI:
10.1016/0014-5793(90)80368-s
[Indexed for MEDLINE]
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