Syrian hamster prion protein

Monte Carlo/simulated annealing (MC/SA) algorithm for sequential assignment in uniformly 13C, 15N-labeled proteins [137]. The two-dimensional (2D) NCACX and NCOCX spectra measured for the fibril samples of full-length Syrian hamster prion protein (residues 23-231) have been analyzed by the MC/SA protocol, from which it has been concluded that the fibril core is formed primarily in the region of residues 173-224 [54]. 

Sokolowski, F., Modler, A. J., Masuch, R., Zirwer, D., Baier, M., Lutsch, G., Moss, D. A., Gast, K., and Naumann, D. (2003). Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein. / Biol. Chem. 278, 40481-40492. 

Liu H, Larr-Jones S, Ulyanov NB et al (1999) Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry 38 5362-5377... 

Fig. 8. Cartoons of three-dimensional PrP structures. (A) Intact recombinant bovine prion protein, bPrP(23-230). (B) Intact recombinant human prion protein, hPrP(23-230). (C) Recombinant Syrian hamster prion protein, shPrP(29-231). The helices are colored green in (A), red in (B) and pink in (C) in all three structures the P strands are cyan, the segments with nonregular secondary structure within the globular domain are yellow, and the residues 23-120 in (A) and (B), and 29-124 in (C) of the flexibly disordered tail are schematically represented by yellow dots.

II. The NMR Structures oe the Recombinant Bovine, Human, Mouse, and Syrian Hamster Prion Proteins... 

Rogers, M., Serban, D., Gyuris, T., Scott, M., Torchia, T, and Prusiner, S.B. (1991). Epitope mapping of the Syrian hamster prion protein utilizing chimeric and mutant genes in a vaccinia virus expression system./. Immunol. 147, 3568-3574. 

Syrian hamster prion protein j /zaPrP(90-231), and found a metastable intermediate conformer of PrP°(PrP ) in which helices B and C are preferentially disordered. They found that the intermediate PrP coexists with normal PrP at a population of 1% under a closely physiological condition (pH 5.2 and 30°C). Kremer et investigated the pressure dependence of two isoforms of the human prion protein. They had to carry out TROSY experiments developed for high-molecular-... 

Weiss, S., Famulok, M., Edenhofer, F, Wang, Y.H., Jones, I.M., Groschup, M., and Win-nacker, E.L. (1995). Overexpression of active Syrian golden hamster prion protein PrPc as a glutathione S-transferase fusion in heterologous systems. J. Virol. 69, 4776-4783. 

Weiss, S., Rieger, R., Edenhofer, F, Fisch, E., and Winnacker, E.-L. (1996). Recombinant prion protein rPrP27-30 from Syrian Golden Hamster reveals proteinase Ksensitivity. Biochem. Biophys. Res. Commun. 219, 173—179. 

Prion diseases seem to arise from an aberrant isoform of a normal cellular prion protein, designated PrP -. The aberrant isoform, designated ftP, differs from the normal protein in its conformation, and the weight of evidence now indicates that a transmissible prion consists exclusively of PrP. No nucleic acid is present, as shown by the fact that infectivity is unaf-f ted by all procedmes that specifically modify nucleic aci moreover, no candidate TSE-specific polynucleotide has ever been found. PrP - and PrP have been purified from the brains of healthy and scrapie-infected Syrian hamsters, respectively. PrP is also called the SAF isoform from its ability to aggregate into rapie-Associated Hbrils. 

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