Prion protein: Difference between revisions
Kurt Giles (talk | contribs) No edit summary |
Kurt Giles (talk | contribs) No edit summary |
||
| Line 14: | Line 14: | ||
==Models of PrP<sup>Sc</sup> structure== | ==Models of PrP<sup>Sc</sup> structure== | ||
Fourier transform infrared (FTIR) spectroscopy, and circular dichroism (CD) studies first demonstrated that PrP<sup>Sc</sup> had very different proportions of α-helices and β-sheet to PrP<sup>C</sup><ref>Pan, KM ''et al.'' (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins ''Proc. Natl. Acad. Sci. USA'' '''90''', 10962-10966</ref>. There are a number of technical obstacles in determining the atomic resolution structure of PrP(sup)Sc</sup>, and the most detailed information to date has been obtained by electron microscopy of 2D crystals<ref>Wille H ''et al.'' (2002) Structural studies of the scrapie prion protein by electron crystallography ''Proc. Natl. Acad. Sci. USA'' '''99''', 3563-3568</ref>. Analysis of 2D crystals binding specific heavy metal ions, and of redacted constructs of PrP, provide a basis for structural modeling. | Fourier transform infrared (FTIR) spectroscopy, and circular dichroism (CD) studies first demonstrated that PrP<sup>Sc</sup> had very different proportions of α-helices and β-sheet to PrP<sup>C</sup><ref>Pan, KM ''et al.'' (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins ''Proc. Natl. Acad. Sci. USA'' '''90''', 10962-10966</ref>. There are a number of technical obstacles in determining the atomic resolution structure of PrP(sup)Sc</sup>, and the most detailed information to date has been obtained by electron microscopy of 2D crystals<ref>Wille H ''et al.'' (2002) Structural studies of the scrapie prion protein by electron crystallography ''Proc. Natl. Acad. Sci. USA'' '''99''', 3563-3568</ref>. Analysis of 2D crystals binding specific heavy metal ions, and of redacted constructs of PrP, provide a basis for structural modeling. | ||
A model the N-terminal region and part of the C-terminal domain, up to the disulphide bond, refolds into a β-helical structure<ref>Govaerts C ''et al.'' (2004) Ecidence for assembly of prions with left-handed β-helices into trimers ''Proc. Natl. Acad. Sci. USA'' '''101''', 8342-8347<ref>. Support for this β-helical model comes from the structure of the fungal prion Het-s ([[2rnm]]). | A model the N-terminal region and part of the C-terminal domain, up to the disulphide bond, refolds into a β-helical structure<ref>Govaerts C ''et al.'' (2004) Ecidence for assembly of prions with left-handed β-helices into trimers ''Proc. Natl. Acad. Sci. USA'' '''101''', 8342-8347</ref>. Support for this β-helical model comes from the structure of the fungal prion Het-s ([[2rnm]]). | ||
==Prion strains== | ==Prion strains== | ||