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Worth a thousand words: Hopkins researchers paint picture of cancer-promoting culprit
Date:1/4/2008

erfered with the way PIK3CA interacted with other proteins and parts of the cell and therefore must be on the outside surface of the enzyme. However, their results show that nearly all the mutations map to regions within the enzyme. Somehow, these internal mutations must cause the protein to subtly change how it works and interacts with itself, says Amzel. Its an interesting problem to solve, trying to figure out what slight shape and structural changes can make an enzyme work better-usually were trying to figure out why things stop working.

The team currently is unraveling the structure of mutated PIK3CA so that they can compare mutated to unmutated to better understand how the mutations lead to cancer. Another goal is to find drugs that can specifically interfere with PIK3CA and turn it down, to develop cancer-fighting therapies.


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Contact: Audrey Huang
audrey@jhmi.edu
410-614-5105
Johns Hopkins Medical Institutions
Source:Eurekalert

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