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- W3004903594 abstract "The oncoprotein E5 from papilloma virus can activate the platelet derived growth factor β receptor (PDGFβR) in the membrane through an interaction of the transmembrane helices. This triggers the signal cascade in a ligand-independent manner, leading to pathogenic growth and cancer. However, is not yet known how the E5 and the PDGFβR interact with each other. Therefore, we aim at getting insight into the structure of this oligomeric complex and condition for its self-assembly using solid-state NMR measurements of inter-molecular distances. Unlike most other structural biological methods, solid-state NMR allows to study oligomeric complexes in a native-like membrane environment, which is required to correctly represent the oligomeric structures. Here, REDOR is one of the most commonly used NMR technologies and is employed for distance measurements between two different spins. Selective 13C-, 15N-, 19F- or 2H-labels were introduced into specific residues that are predicted to be located at the interface between E5 and PDGFβR. Putative contact pairs were measured under suitable conditions in which two proteins approach each other. So far, the distances we measured have verified several proposed contacts between E5 and PDGFβR, like between F28 in E5 and L506 in PDGFβR, or between L24 and L509. This way, our results help to understand the mechanism of how E5 activates PDGFβR and provide important clues for future drug development." @default.
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- W3004903594 date "2020-02-01" @default.
- W3004903594 modified "2023-09-26" @default.
- W3004903594 title "Self-Assembly of E5/PDGFβR in Membranes Studied by Solid-State NMR Distance Measurements" @default.
- W3004903594 doi "https://doi.org/10.1016/j.bpj.2019.11.1254" @default.
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