Pregled bibliografske jedinice broj: 506854
NMR structure of the human prion protein with the pathological Q212P mutation
NMR structure of the human prion protein with the pathological Q212P mutation // Magnetic Moments in Central Europe / Liptaj, Tibor ; Imrich, Jan ; Kovalakova, Maria ; Olčak, Dušan (ur.).
Vysoké Tatry: Slovak National NMR Centre, Slovak Chemical Society, 2011. str. 46-46 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 506854 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
NMR structure of the human prion protein with the pathological Q212P mutation
Autori
Ilc, Gregor ; Giachin, Gabriele ; Biljan, Ivana ; Zhukov, Igor ; Legname, Giuseppe ; Plavec, Janez
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Magnetic Moments in Central Europe
/ Liptaj, Tibor ; Imrich, Jan ; Kovalakova, Maria ; Olčak, Dušan - Vysoké Tatry : Slovak National NMR Centre, Slovak Chemical Society, 2011, 46-46
ISBN
978-80-89284-77-1
Skup
Magnetic Moments in Central Europe
Mjesto i datum
Vysoké Tatry, Slovačka, 16.03.2011. - 20.03.2011
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
NMR; human prion protein; inherited prion diseases; Q212P mutant
Sažetak
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are fatal neurodegenerative disorders associated with the conversion of a normal (cellular) prion protein, PrPC, into a misfolded isoform, PrPSc. According to the "protein-only hypothesis" PrPSc itself is the infectious TSE pathogen. One of the strongest arguments supporting this hypothesis is the link between inherited prion diseases and mutations in the gene coding for human PrP. Several point mutations leading to familial prion diseases have been identified in PRNP gene but largely still unknown is how these mutations affect the transition of PrPC to PrPSc. Structural studies on PrP variants carrying familial mutations, more prone to spontaneous conversion into the infectious form, may be an important step toward understanding the molecular mechanism at early stages of the disease. In the current study we have determined a high-resolution 3D structure of the truncated recombinant HuPrP(90-231) with the pathological Q212P mutation that is associated with a Gerstmann-Sträussler-Scheinker (GSS) syndrome. The structure of Q212P mutant reveals unique structural features in comparison to the known wild-type PrP structures. The most remarkable differences involve the C-terminal end of the protein and the β2-α2 loop region. The spontaneous generation of PrPSc in familial cases might be due to the disruptions of the hydrophobic core consisting of β2-α2 loop and α3 helix.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
