Abstract:
:Three site-directed mutants of human epidermal growth factor, Leu-26----Gly, Leu-47----Ala, and Ile-23----Thr, were examined for their ability to stimulate the protein-tyrosine kinase activity of the epidermal growth factor receptor. The receptor binding affinities of the mutant growth factors were 20- to 50-fold lower, as compared to wild-type growth factor. At saturating concentrations of growth factor, the velocities of the phosphorylation of exogenously added substrate and receptor autophosphorylation were significantly lower with the mutant analogs, suggesting a partial 'uncoupling' of signal transduction. The mutant analogs were shown to compete directly with the binding of wild-type, resulting in a decrease in growth factor-stimulated kinase activity.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Matsunami RK,Campion SR,Niyogi SK,Stevens Adoi
10.1016/0014-5793(90)80776-fsubject
Has Abstractpub_date
1990-05-07 00:00:00pages
105-8issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(90)80776-Fjournal_volume
264pub_type
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