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Molecule Serves as a Key in Some Protein Interactions
Date:11/4/2011

the pocket indicate it might be a completely new route to generating small- molecule inhibitors," Schulman said. Pharmaceutical companies are already targeting other parts of the same NEDD8 pathway, and one experimental drug has entered clinical trials.

Not only does Ubc12's acetylated tail fit perfectly into the pocket, but acetylation solved another problem that would have made the interaction of Ubc12 and Dcn1 difficult. Without acetylation, Ubc12 and the Dcn1 pocket would repel each other much like oil and water. Acetylation neutralizes the charge on Ubc12, allowing the interaction to occur, Schulman said.

Other authors are Julie Monda of St. Jude; J. Wade Harper of Harvard Medical School; and Eric Bennett, formerly of Harvard Medical School and now at University of California, San Diego.

The research was funded in part by the National Institutes of Health, Howard Hughes Medical Institute, Millennium Pharmaceuticals, Damon Runyon Cancer Research Foundation and ALSAC.

St. Jude Children's Research Hospital

St. Jude Children's Research Hospital is internationally recognized for its pioneering research and treatment of children with cancer and other life-threatening diseases. The hospital's research has helped push overall survival rates for childhood cancer from less than 20 percent when the institution opened to almost 80 percent today. It is the first and only National Cancer Institute-designated Comprehensive Cancer Center devoted solely to children, and no family ever pays St. Jude for care. For more information, visit www.stjude.org

 


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SOURCE St. Jude Children's Research Hospital
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