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Structure‐function analysis of epidermal growth factor: site directed mutagenesis and nuclear magnetic resonance
Author(s) -
Dudgeon T.J.,
Cooke R.M.,
Baron M.,
Campbell I.D.,
Edwards R.M.,
Fallon A.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80600-n
Subject(s) - mutagenesis , function (biology) , nuclear magnetic resonance , chemistry , epidermal growth factor , site directed mutagenesis , magnetic resonance imaging , microbiology and biotechnology , biophysics , mutation , biology , biochemistry , physics , mutant , medicine , gene , receptor , radiology
The role of leucine‐47 in determining the structure and activity of human epidermal growth factor was examined using site‐directed mutagenesis. Wild type protein and four variants in which Leu 47 was replaced by valine, glutamate, aspartate and alanine were produced from yeast. 1 H NMR experiments demonstrated that substitution of Leu 47 had little effect on the protein structure. The observed reduction in receptor binding affinity caused by the substitutions could thus be attributed to perturbation of a residue directly involved in receptor interactions.