Human prion protein structure

Walsh P, Simonetti K, Sharpe S (2009) Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein. Structure 17 417 -26... 

Zahn R, Liu A, Luhrs T et al (2000) NMR solution structure of the human prion protein. Proc Natl Acad Sci USA 97 145-150... 

Fig. 1 Diagram of the human prion protein gene showing the octapeptide repeat region (51-91), regions of predicted secondary structure [designated a (helical) or [3 (sheet)], pathogenic or likely pathogenic mutations (above in red), non-synonymous polymorphisms and synonymous polymorphisms (below in green)...

Zhang Y, Swietnicki W, Zagorski MG et al (2000) Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion... 

Knaus KJ, Morillas M, Swietnicki W et al (2001) Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat Struct Biol 8 770-774... 

Antonyuk SV, Trevitt CR, Strange RW et al (2009) Crystal structure of human prion protein bound to a therapeutic antibody. Proc Natl Acad Sci USA 106 2554-2558... 

Calzolai L, Zahn R (2003) Influence of pH on NMR structure and stability of the human prion protein globular domain. J Biol Chem 278 35592-35596... 

Cobb NJ, Sonnichsen FD, Mchaourab H et al (2007) Molecular architecture of human prion protein amyloid a parallel, in-register (3-structure. Proc Natl Acad Sci USA 104 18946-18951... 

Fig. I Structure of the human prion protein, (a) The mature human prion protein as it can be found on the outer cell membrane. The GPI-anchor (attached to Ser230) and typical glycans (attached to Asnl81 and Asnl97) are shown in sticks. Structure obtained from MD simulation (Van der Kamp, Koldsp and Daggett, unpublished results), (b) The structured part of the recombinant human prion protein, as obtained by protein NMR [39]. Secondary structure elements are labeled...

Jackson GS, Hill SF, Joseph C, HosszuL, Power A, Waltho JP, Clarke AR, Collinge J (1999) Multiple folding pathways for heterologously expressed human prion protein. Biochim Biophys Acta Protein Structure and Molecular Enzymology 1431 1... 

Hosszu LLP, Baxter NJ, Jackson GS, Power A, Clarke AR, Waltho JP, Craven CJ, Collinge J (1999) Structural mobility of the human prion protein probed by backbone hydrogen exchange. Nat Struct Biol 6 740... 

Rossetti G, Giachin G, Legname G, Carloni P (2010) Structural facets of disease-linked human prion protein mutants a molecular dynamic study. Proteins Struct Funct Bioinform, doi 10.1002/prot.22834... 

Van der Kamp MW, Daggett V (2010) Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding. J Mol Biol 404 732... 

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.

Morillas, M., Swietnicki, W., Gambetti, P. and Surewicz, W.K., Membrane environment alters the conformational structure of the recombinant human prion protein, J Biol Chem 274 (1999) 36859-36865. 

Fig. 9. Ribbon representation of the NMR structure of the human prion protein isoform /i PrP(121-230) (taken from PDB 1QM2). Residues conferring to the fast process with molar free energy values at ambient pressure (AGq) of about 3.2kJ/mol are coloured blue (A) and residues involved in the slow process with molar free energy values at ambient pressure (AGo) of about 14.2 kJ/mol coloured orange and red (B). Residues with very low-pressure stability (A Go lower than the mean value plus one standard deviation) are coloured red. Cavities were calculated using a probe radius of 0.12nm. (After ref 46.)...

Inadequate crystallinity in the amyloid deposits of the PrP form of human prion protein or of any of its mutated and truncated forms limits the details of the p-structure available from X-ray crystallography. A recent report of electron crystallography of two-dimensional crystals of the proteinase K-treated PrP form giving essentially the sequence from residues 90 to 231, however, is available. The model focusing on the P-structure appears in top view in Figure 7.36A and in side view in Figure 7.36B. The... 

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