Pregled bibliografske jedinice broj: 506852
NMR studies of human prion proteins with pathological mutations
NMR studies of human prion proteins with pathological mutations // 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. 28-28 (predavanje, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 506852 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
NMR studies of human prion proteins with pathological mutations
Autori
Biljan, Ivana ; Ilc, Gregor ; Giachin, Gabriele ; 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, 28-28
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
Predavanje
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
NMR; human prion protein; inherited prion diseases; Q212P mutant
Sažetak
Prion diseases belong to a group of fatal neurodegenerative disorders caused by the conversion of the normal cellular prion protein (PrPC) into its pathogenic form (PrPSc). According to the "protein-only hypothesis" PrPSc is the sole component of the infectious agents. One of the key arguments supporting this hypothesis is the link between inherited prion diseases and mutations in the gene coding for human PrP. Several pathogenic mutations leading to familial prion diseases have been identified in the prion protein gene (PRNP) open reading frame. However, it is still largely unknown how these mutations affect the PrPC→PrPSc conversion. Structural studies on PrP variants carrying familial mutations may provide new clues about 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) containing the pathological Q212P mutation that is associated with a Gerstmann-Sträussler-Scheinker (GSS) syndrome. In comparison to the other known PrP structures, structure of Q212P mutant shows some unique structural features. The most remarkable differences involve the C-terminal end of the protein and the β2-α2 loop. Spontaneous generation of PrPSc in inherited prion diseases might be due to the disruptions of the hydrophobic core consisting of β2-α2 loop and α3 helix.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
