Abstract
Abstract Cisplatin resistance is notorious in leading to therapeutic failure of many solid malignancies. Various resistance mechanisms have been proposed while many more are being added, based on the growing number of resistance-inducing genes identified. TMEM205 is an integral membrane protein with unknown function, but its intracellular level was found markedly elevated in cisplatin resistance cells, the mechanism of which is unknown. Here for the first time we characterized the molecular mechanism of TMEM205-mediated cisplatin resistance through structural and functional studies of TMEM205. The crystal structure of the full-length TMEM205 was obtained at 2.5 Å resolution and shows a 4-helix bundle with a highly hydrophilic tunnel. Strong anomalous signals were observed indicating platinum binding sites. Our structural and functional study of TMEM205 provides novel insight into the complexity of cisplatin resistance. Citation Format: Xiaoyun Bai, Di Xia. Structural characterization of transmembrane protein TMEM205 [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2019; 2019 Mar 29-Apr 3; Atlanta, GA. Philadelphia (PA): AACR; Cancer Res 2019;79(13 Suppl):Abstract nr 2112.
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