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Crystal Structures of Polymorphic Prion Protein β1 Peptides Reveal Variable Steric Zipper Conformations.

Yu L, Lee SJ, Yee VC
Biochemistry 54 3640-8 (2015)
Related entries: 4tut, 4uby, 4ubz, 4w5l, 4w5m, 4w5y, 4w67, 4w71, 4wbu, 4wbv

Cited: 11 times
EuropePMC logo PMID: 25978088

Abstract

The pathogenesis of prion diseases is associated with the conformational conversion of normal, predominantly α-helical prion protein (PrP(C)) into a pathogenic form that is enriched with β-sheets (PrP(Sc)). Several PrP(C) crystal structures have revealed β1-mediated intermolecular sheets, suggesting that the β1 strand may contribute to a possible initiation site for β-sheet-mediated PrP(Sc) propagation. This β1 strand contains the polymorphic residue 129 that influences disease susceptibility and phenotype. To investigate the effect of the residue 129 polymorphism on the conformation of amyloid-like continuous β-sheets formed by β1, crystal structures of β1 peptides containing each of the polymorphic residues were determined. To probe the conformational influence of the peptide construct design, four different lengths of β1 peptides were studied. From the 12 peptides studied, 11 yielded crystal structures ranging in resolution from 0.9 to 1.4 Å. This ensemble of β1 crystal structures reveals conformational differences that are influenced by both the nature of the polymorphic residue and the extent of the peptide construct, indicating that comprehensive studies in which peptide constructs vary are a more rigorous approach to surveying conformational possibilities.

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  2. Tailoring pore distribution in polymer films via evaporation induced phase separation. Pervin R, Ghosh P, Basavaraj MG. RSC Adv 9 15593-15605 (2019)


Reviews citing this publication (1)

  1. Toward the Atomic Structure of PrPSc. Rodriguez JA, Jiang L, Eisenberg DS. Cold Spring Harb Perspect Biol 9 a031336 (2017)

Articles citing this publication (8)

  1. Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity. Krotee P, Rodriguez JA, Sawaya MR, Cascio D, Reyes FE, Shi D, Hattne J, Nannenga BL, Oskarsson ME, Philipp S, Griner S, Jiang L, Glabe CG, Westermark GT, Gonen T, Eisenberg DS. Elife 6 e19273 (2017)
  2. Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities. Louros N, Orlando G, De Vleeschouwer M, Rousseau F, Schymkowitz J. Nat Commun 11 3314 (2020)
  3. Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion. Abskharon R, Wang F, Wohlkonig A, Ruan J, Soror S, Giachin G, Pardon E, Zou W, Legname G, Ma J, Steyaert J. PLoS Pathog 15 e1008139 (2019)
  4. Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease. Zheng Z, Zhang M, Wang Y, Ma R, Guo C, Feng L, Wu J, Yao H, Lin D. Sci Rep 8 13211 (2018)
  5. Protective V127 prion variant prevents prion disease by interrupting the formation of dimer and fibril from molecular dynamics simulations. Zhou S, Shi D, Liu X, Liu H, Yao X. Sci Rep 6 21804 (2016)
  6. In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model. Roterman I, Stapor K, Fabian P, Konieczny L. Int J Mol Sci 22 10587 (2021)
  7. A fluorogenic probe for granzyme B enables in-biopsy evaluation and screening of response to anticancer immunotherapies. Scott JI, Mendive-Tapia L, Gordon D, Barth ND, Thompson EJ, Cheng Z, Taggart D, Kitamura T, Bravo-Blas A, Roberts EW, Juarez-Jimenez J, Michel J, Piet B, de Vries IJ, Verdoes M, Dawson J, Carragher NO, Connor RAO, Akram AR, Frame M, Serrels A, Vendrell M. Nat Commun 13 2366 (2022)
  8. The polar clasps of a bank vole PrP(168-176) prion protofibril revisiting. Zhang J. J Mol Model 25 108 (2019)


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