Structural Biology

Seeing the clasps that stabilize prion fibrils

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Science  13 Apr 2018:
Vol. 360, Issue 6385, pp. 167-168
DOI: 10.1126/science.360.6385.167-f

A cryo–electron microscopy method called MicroED (micro–electron diffraction) has been used to reveal the core structures of several amyloid fibrils. With this technique, Gallagher-Jones et al. determined a 0.72-Å-resolution structure of fibrils formed by a peptide at the core of the infectious scrapie form of mammalian prion protein (proto-PrPSc). Like the full PrPSc, the fibril is characterized by unusually high stability. The high-resolution structure shows β-strands that stack into β-sheets, with sheets pairing front-to-back to form fibrils. A network of hydrogen bonds within and between β-strands forms “polar clasps,” which are shielded by aromatic residues that stack in the fibrils.

Nat. Struct. Mol. Biol. 25, 131 (2018).

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