Structure of key breast cancer receptor determined

e difference for HER2. Specifically, HER2 doesn't need to be "opened" before it can pair with another HER, which is why extra HER2 can cause cancer, and why no one has found any small molecules, or ligands, that bind to it, Leahy says.

"We can see now that it's unlikely any natural ligands for HER2 exist -- it just doesn't need one to work," says Leahy.

Led by postdoctoral fellow Hyun-Soo Cho, the research team grew crystals of the extracellular region of the HER2 protein, provided by scientists at Genitope Corporation in California. After bombarding the crystals with radiation at the National Synchnotron Light Source at Brookhaven National Lab on Long Island, N.Y., Cho and Leahy interpreted the data to create the protein's structure. The team did the same with crystals of HER2 bound to Herceptin antibody.

The extracellular regions of all the HER proteins are made up of four structurally distinct "domains," I, II, III and IV. In HER1 and 3, a fingerlike projection in domain II keeps it connected to domain IV, forming a bracelet-like loop. In HER2, however, a tight interaction between domains I and III, which Leahy likens to a spot weld, prevents the bracelet formation. Thus domain IV is available for binding to Herceptin, and domain II for pairing with other HER proteins. (See accompanying image.)


Contact: Joanna Downer
Johns Hopkins Medical Institutions

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