NR AMGF
AU Warwicker,J.
TI Species barriers in a model for specific prion protein dimerisation
QU Biochemical and Biophysical Research Communications 1997 Mar 17; 232(2): 508-12
PT journal article
AB It has been proposed that the most highly conserved sequence segment within the prion protein (PrP) may be involved in dimer formation within both the normal (PrPc) and misfolded (PrPsc) forms. This hypothesis is now examined in the context of amino acids known to be involved in species barriers or in disease modifying polymorphisms, and the structure of a mouse PrP fragment. These locations can be plausibly explained on the basis of the specific dimer model, so that a potential role for a conserved dimerisation element in prion disease progression cannot be excluded.
MH Animal; Dimerization; Disease Susceptibility; Haplorhini; Human; Mice; *Models, Molecular; Polymorphism (Genetics); Prion Diseases/genetics/metabolism/transmission; Prions/*chemistry/*genetics/metabolism; Protein Conformation; Species Specificity; Support, Non-U.S. Gov't
AD Institute of Food Research, Reading Laboratory, United Kingdom.
SP englisch
PO USA