Abstract
Breast cancer has several defining prognostic and predictive markers, one of which is HER‐2. The Human Epidermal Growth Factor Receptor (HER‐2) is a protein which plays a role in cellular proliferation and cell survival. The solved structure revealed that the protein has an extracellular ligand binding domain. However, HER‐2 has no known ligand to bind to its active site. Consequently, its known function is to dimerize with its sister receptor (HER‐3) and initiate a cascade pathway for growth. The upregulation of the HER‐2 neu oncogene can result in the overexpression of HER‐2, causing a change in the ratio of HER‐2 to HER‐3 receptors. Because HER‐2 promotes cellular proliferation and survival, uncontrolled expression of this factor has major implications in carcinogenesis. About twenty percent of all breast cancers are diagnosed as HER‐2 positive. Treatments to inhibit HER‐2 include ligand mimetics which bind to HER‐2, preventing its dimerization with HER‐3 and therefore stopping the uncontrolled cellular proliferation that would otherwise occur downstream. The FDA has approved several anti‐HER2 antibody therapies which have been used in combination with chemotherapy in the adjuvant and neoadjuvant setting. Trastuzumab (Herceptin) and Pertuzumab (Perjeta) are two anti‐HER2 antibodies which, in conjunction with chemotherapy, have resulted in improved outcomes for HER‐2 positive breast cancer patients. The Walton High School MSOE Center for BioMolecular Modeling SMART Team used 3‐D modeling and printing technology to examine the structure‐function relationship between HER‐2 as it relates to carcinogenesis.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Published Version
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