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Nmr structure of a variant human prion protein with two disulfide bridges

Academic Article
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Overview

authors

  • Zahn, R.
  • Guntert, P.
  • von Schroetter, C.
  • Wuthrich, Kurt

publication date

  • February 2003

journal

  • Journal of Molecular Biology  Journal

abstract

  • The nuclear magnetic resonance structure of the globular domain with residues 121-230 of a variant human prion protein with two disulfide bonds, hPrP(M166C/E221C), shows the same global fold as wild-type hPrP(121-230). It contains three alpha-helices of residues 144-154, 173-194 and 200-228, an anti-parallel beta-sheet of residues 128-131 and 161-164, and the disulfides Cys166-Cys221 and Cys179-Cys214. The engineered extra disulfide bond in the presumed "protein X"-binding site is accommodated with slight, strictly localized conformational changes. High compatibility of hPrP with insertion of a second disulfide bridge in the protein X epitope was further substantiated by model calculations with additional variant structures. The ease with which the hPrP structure can accommodate a variety of locations for a second disulfide bond within the presumed protein X-binding epitope suggests a functional role for the extensive perturbation by a natural second disulfide bond of the corresponding region in the human doppel protein.

subject areas

  • Amino Acid Sequence
  • Disulfides
  • GPI-Linked Proteins
  • Genetic Variation
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Prions
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Software
  • Thermodynamics
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Research

keywords

  • NMR structure
  • disulfide bonds
  • doppel protein
  • prion protein
  • protein X epitope
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/s0022-2836(02)01332-3

PubMed ID

  • 12547204
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Additional Document Info

start page

  • 225

end page

  • 234

volume

  • 326

issue

  • 1

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