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Atomic  resolution (2.3 Å) model derived from cryo-EM structure of the p97 hexamer with allosteric inhibitors bound at the junction between the D1 and D2 domains.

Atomic resolution (2.3 Å) model derived from cryo-EM structure of the p97 hexamer with allosteric inhibitors bound at the junction between the D1 and D2 domains.

p97 is a protein that plays a role in maintaining protein quality and is an attractive target for cancer therapy. A paper published online in Science on January 28, 2016 (Banerjee et al., 2016) reports the high resolution cryo-EM structures for full-length, hexameric p97 in the presence and absence of a novel allosteric inhibitor developed by a collaborative team of academic scientists participating in the NCI Chemical Biology Consortium.

Members of the cryo-EM project team included scientists from the following institutions:

The Laboratory of Cell Biology, NCI, Bethesda, MD
Small Molecule Discovery Center, University of California, San Francisco
Chemical Diversity Center, University of Pittsburgh Pittsburgh, PA
Leidos Biomedical Research Inc., Frederick, MD
Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA

Reference: Banerjee et al., 2016. 2.3 Å resolution cryo-EM structure of human p97 and mechanism of allosteric inhibition. Science. Online January 28, 2016.

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