Article
An intact Raf zinc finger is required for optimal binding to processed Ras and for ras-dependent Raf activation in situ.
Molecular and cellular biology - 1 Jan 1997
Luo Z, Diaz B, Marshall M S, Avruch J
Abstract excerpt
The function of the c-Raf-1 zinc finger domain in the activation of the Raf kinase was examined by the creation of variant zinc finger structures. Mutation of Raf Cys 165 and Cys 168 to Ser strongly inhibits the Ras-dependent activation of c-Raf-1 by epidermal growth factor (EGF). Deletion of the Raf zinc finger and replacement with a homologous zinc finger from protein kinase C gamma (PKC gamma) (to give...
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