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Prion protein-detergent micelle interactions studied by NMR in solution

Academic Article
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Overview

authors

  • Hornemann, S.
  • von Schroetter, C.
  • Damberger, F. F.
  • Wuthrich, Kurt

publication date

  • August 2009

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Cellular prion proteins, PrP(C), carrying the amino acid substitutions P102L, P105L, or A117V, which confer increased susceptibility to human transmissible spongiform encephalopathies, are known to form structures that include transmembrane polypeptide segments. Herein, we investigated the interactions between dodecylphosphocholine micelles and the polypeptide fragments 90-231 of the recombinant mouse PrP variants carrying the amino acid replacements P102L, P105L, A117V, A113V/A115V/A118V, K110I/H111I, M129V, P105L/M129V, and A117V/M129V. Wild-type mPrP-(90-231) and mPrP[M129V]-(91-231) showed only weak interactions with dodecylphosphocholine micelles in aqueous solution at pH 7.0, whereas discrete interaction sites within the polypeptide segment 102-127 were identified for all other aforementioned mPrP variants by NMR chemical shift mapping. These model studies thus provide evidence that amino acid substitutions within the polypeptide segment 102-127 affect the interactions of PrP(C) with membranous structures, which might in turn modulate the physiological function of the protein in health and disease.

subject areas

  • Amino Acid Sequence
  • Animals
  • Detergents
  • Magnetic Resonance Spectroscopy
  • Mice
  • Micelles
  • Molecular Sequence Data
  • Phosphorylcholine
  • Prions
  • Sequence Homology, Amino Acid
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Identity

PubMed Central ID

  • PMC2755680

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M109.000430

PubMed ID

  • 19546219
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Additional Document Info

start page

  • 22713

end page

  • 22721

volume

  • 284

issue

  • 34

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