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Lab, Field, & Clinic |

New Compound Inhibits Elusive Protein Behind Many Cancers

Tracy Hampton, PhD
JAMA. 2014;311(2):127. doi:10.1001/jama.2013.284385.
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With the ongoing development of targeted therapies, numerous abnormal proteins that play key roles in cancer development and progression have been neutralized by drugs that inhibit their activity. But some, like the Ras family of proteins, have proven difficult to overcome and in some cases have even been considered “undruggable.”

That pessimism appears to be waning, however, in the face of intense interest in cracking Ras proteins’ ability to resist drugs designed to block them. Last June, the National Cancer Institute (NCI) announced that it will devote $10 million to an effort that will bring extramural researchers together to collaborate on new strategies to target RAS oncogenes (http://1.usa.gov/1jGWSQu).

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A mutant form of the K-Ras protein is a powerful driver of cancer. A potentially therapeutic compound binds in a pocket of this protein, irreversibly attaches to the mutated amino acid—a cysteine (yellow) that had been substituted for a glycine—and destabilizes the interaction between K-Ras and guanosine triphosphate. This keeps the protein in an inactive state, preferentially binding to guanosine diphosphate (GDP).

Jonathan M. Ostrem, PhD/University of California, San Francisco

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