PRIO

Event=Alternative initiation; Named isoforms=2; Name=1; Synonyms=PrP; IsoId=P04156-1; Sequence=Displayed; Name=3; Synonyms=AltPrP; IsoId=F7VJQ1-1; Sequence=External

63..67; 70..73; 79..82; 92..95; 99..101; 109..112; 118..122; 125..127; 128..131; 133..135; 138..140; 141..143; 159..163; 178..181; 182..185; 189..192; 196..202; 205..210; 212..215

The normal, monomeric form, PRPN(C), has a mainly alpha-helical structure. Misfolding of this form produces a disease-associated, protease-resistant form, PRPN (Sc), accompanied by a large increase of the beta-sheet content and formation of amyloid fibrils. These fibrils consist of a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization. In addition, the heparan-sulfate proteoglycan, GPC1, promotes the association of PRPN (C) to lipid rafts and appears to facilitate the conversion to PRPN (Sc).; DOMAIN: Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization.

23..230; Interaction with GRB2, ERI3 and SYN1; 23..38; Interaction with ADGRG6; 26..108; Disordered; 51..91; 5 X 8 AA tandem repeats of P-H-G-G-G-W-G-Q