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• W2081567318 abstract "p185(her2/neu) belongs to the ErbB receptor tyrosine kinase family, which has been associated with human breast, ovarian, and lung cancers. Targeted therapies employing ectodomain-specific p185(her2/neu) monoclonal antibodies (mAbs) have demonstrated clinical efficacy for breast cancer. Our previous studies have shown that p185(her2/neu) mAbs are able to disable the kinase activity of homomeric and heteromeric kinase complexes and induce the conversion of the malignant to normal phenotype. We previously developed a chimeric antibody chA21 that specifically inhibits the growth of p185(her2/neu)-overexpressing cancer cells in vitro and in vivo. Herein, we report the crystal structure of the single-chain Fv of chA21 in complex with an N-terminal fragment of p185(her2/neu), which reveals that chA21 binds a region opposite to the dimerization interface, indicating that chA21 does not directly disrupt the dimerization. In contrast, the bivalent chA21 leads to internalization and down-regulation of p185(her2/neu). We propose a structure-based model in which chA21 cross-links two p185(her2/neu) molecules on separate homo- or heterodimers to form a large oligomer in the cell membrane. This model reveals a mechanism for mAbs to drive the receptors into the internalization/degradation path from the inactive hypophosphorylated tetramers formed dynamically by active dimers during a physiologic process." @default.
• W2081567318 created "2016-06-24" @default.
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• W2081567318 date "2011-09-01" @default.
• W2081567318 modified "2023-09-29" @default.
• W2081567318 title "Structural Insights into the Down-regulation of Overexpressed p185 Protein of Transformed Cells by the Antibody chA21" @default.
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• W2081567318 doi "https://doi.org/10.1074/jbc.m111.235184" @default.
• W2081567318 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3173138" @default.
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