Document Detail

Aromaticity at position 37 in human epidermal growth factor is not obligatory for activity.
MedLine Citation:
PMID:  1850095     Owner:  NLM     Status:  MEDLINE    
The third disulfide loop (amino acids 33 to 42) of human epidermal growth factor (hEGF) encompasses the region of highest amino acid conservation among all of the EGF-like family of molecules. The importance of some of these highly conserved residues for the maintenance of biological activity, especially the aromatic amino acid tyrosine at position 37, has until now been considered essential on the basis of previous studies with the EGF-like molecule transforming growth factor alpha. Variants at the Tyr-37 position of hEGF were constructed by site-directed mutagenesis. The substituting amino acids were phenylalanine, histidine, serine, alanine, aspartic acid, arginine, and glycine. The variants were tested for their ability to competitively displace native [125I]hEGF from its receptor and to stimulate the protein-tyrosine kinase activity of the receptor; the order of efficacy of substituting amino acids was Phe greater than His greater than Ser greater than Ala greater than Asp greater than Arg greater than Gly in both assays. All were effective, with no or only moderate reduction in potency, in stimulating the incorporation of [3H]thymidine into acid-insoluble material of quiescent mouse A31 cells. Only Tyr-37----Ala, Tyr-37----Arg and Tyr-37----Gly were slightly less potent in the cell assay. Thus, neither tyrosine nor another aromatic amino acid at position 37 in hEGF is essential for full biological activity.
D A Engler; M R Hauser; J S Cook; S K Niyogi
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  11     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  1991 May 
Date Detail:
Created Date:  1991-05-21     Completed Date:  1991-05-21     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2425-31     Citation Subset:  IM    
University of Tennessee-Oak Ridge Graduate School of Biomedical Sciences and the Protein Engineering and Molecular Mutagenesis, Oak Ridge National Laboratory 37831-8077.
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MeSH Terms
Amino Acid Sequence
Base Sequence
Binding, Competitive
Epidermal Growth Factor / genetics*,  metabolism,  pharmacology
Molecular Sequence Data
Mutagenesis, Site-Directed
Oligonucleotide Probes / chemical synthesis
Protein-Tyrosine Kinases / drug effects,  metabolism
Receptor, Epidermal Growth Factor / metabolism
Restriction Mapping
Sequence Homology, Nucleic Acid
Grant Support
Reg. No./Substance:
0/Oligonucleotide Probes; 62229-50-9/Epidermal Growth Factor; EC Kinases; EC, Epidermal Growth Factor

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