Publication: Structural characterization of POM6 Fab and mouse prion protein complex identifies key regions for prions conformational conversion
Structural characterization of POM6 Fab and mouse prion protein complex identifies key regions for prions conformational conversion
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Baral, P. K., Swayampakula, M., Aguzzi, A., & James, M. N. G. (2018). Structural characterization of POM6 Fab and mouse prion protein complex identifies key regions for prions conformational conversion. FEBS Journal, 285(9), 1701–1714. https://doi.org/10.1111/febs.14438
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Conversion of the cellular prion protein PrPC into its pathogenic isoform PrPSc is the hallmark of prion diseases, fatal neurodegenerative diseases affecting many mammalian species including humans. Anti‐prion monoclonal antibodies can arrest the progression of prion diseases by stabilizing the cellular form of the prion protein. Here, we present the crystal structure of the POM6 Fab fragment, in complex with the mouse prion protein (moPrP). The prion epitope of POM6 is in close proximity to the epitope recognized by the purportedly t
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Baral, P. K., Swayampakula, M., Aguzzi, A., & James, M. N. G. (2018). Structural characterization of POM6 Fab and mouse prion protein complex identifies key regions for prions conformational conversion. FEBS Journal, 285(9), 1701–1714. https://doi.org/10.1111/febs.14438