An intact Raf zinc finger is required for optimal binding to processed Ras and for ras-dependent Raf activation in situ.
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 Ra...
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| Published in: | Mol Cell Biol |
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| Main Authors: | , , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
Taylor & Francis
1997
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC231728/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8972184/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.17.1.46 |
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