KRAS insertion mutations are oncogenic and exhibit distinct functional properties
Amino acid substitutions in K-Ras that constitutively activate the protein are common in cancer. Here, the authors describe mutations in the K-RasSwitch 2 domain and show that the mutant proteins accumulate in the active conformation, exhibit defective binding to PI3 kinase, and are hypersensitive t...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2016-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms10647 |