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Default NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment

NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment


Abstract Targeting the receptor for the advanced glycation endproducts (RAGE) signalling has a potential for the prevention and treatment of several pathologies. Extracellular activation of RAGE triggers the interactions of the RAGE cytoplasmic tail with intracellular protein partners. Here the cytoplasmic tail of RAGE has been investigated by NMR as part of the full-length protein, in the presence of a membrane-mimicking environment. The isolated cytoplasmic tail has also been studied for comparison. The NMR spectra of the whole receptor show that some but not all residues belonging to the C-terminal region of the cytoplasmic tail have a large flexibility, while the membrane proximal region seems to be rigidly connected to the trans-membrane domain and ectodomains. The analysis indicates that the behavior of the cytoplasmic tail is strongly affected by its being part of the whole receptor. These results provide new insight towards the understanding of signal transduction by RAGE.
  • Content Type Journal Article
  • Category Article
  • Pages 1-6
  • DOI 10.1007/s10858-012-9671-0
  • Authors
    • Valentina Borsi, Magnetic Resonance Center (CERM), University of Florence, via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
    • Linda Cerofolini, Magnetic Resonance Center (CERM), University of Florence, via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
    • Marco Fragai, Magnetic Resonance Center (CERM), University of Florence, via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
    • Claudio Luchinat, Magnetic Resonance Center (CERM), University of Florence, via L. Sacconi 6, 50019 Sesto Fiorentino, Italy

Source: Journal of Biomolecular NMR
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