Bovine prion protein structure

Lopez Garcia, F., Zahn, R., Riek, R., and Wiithrich, K. (2000). NMR structure of the bovine prion protein. Proc. Natl. Acad. Sci. USA 97, 8334-8339. 

ESiverstahl, H., A. Andersson, A. Graslund and L. Maler (2004) NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein. Biochemistry 43, 14940-14947. 

Homemann S, Schom C, Wuthrich K (2004) NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO Rep 5 1159-1164... 

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.

The normal cellular form of prion protein (PrPc) can exist as a Cu-metalloprotein in vivo (492). This PrPc is a precursor of the pathogenic protease-resistant form PrPsc, which is thought to cause scrapie, bovine spongiform encephalopathy (BSE), and Creutzfeldt—Jakob disease. Two octa-repeats of PHGGGWGQ have been proposed as Cu(II) binding sites centered on histidine (493). They lack secondary and tertiary structure in the absence of Cu(II). Neurons may therefore have special mechanisms to regulate the distribution of copper. 

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

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