PrP^C creates a hydrogel in crowded phisiological conditions with ~12- or ~50-mer Amiloid beta oligomers (Aβo). In the hydrogel PrP^C is moderately to highly mobile, depending on the ratio of Aβo to PrP^C. Aβo seems to be highly coordinated in the gel, and does not show mobility. Major secondary structure changes are observed for hydrogel PrP^C. In monomeric PrP^C, the 40 Gly of the N-term and the six Ala of the linker region (aa 113–120) are unstructured. The vast majority of these residues exhibit a-helical character in the hydrogel. This conformational shift spans PrP^C regions for mGluR5 and Aβo interaction. PrP^C regions 23-51, and 91-111 bind to Aβo (PMID:30401430).
Literature supporting the
LLPS: 30401430
Functional class of membraneless organelle:
not known/not clear