Jiapu Zhang
Prion protein (PrP) has two regions: unstructured region PrP(1-120) and structured region PrP(119-231). In the structured region, there are many segments which have the property of amyloid fibril formation. By theoretical calculations, PrP(126-133), PrP(137-143), PrP(170-175), PrP(177-182), PrP(211-216) have the amyloid fibril forming property. PrP(142-166) has a X-ray crystallography experimental β-hairpin structure, instead of a pure cross-β amyloid fibril structure; thus we cannot clearly find it by our theoretical calculations. However, we can predict that there must be a laboratory X-ray crystal structure in PrP(184-192) segment that will be produced in the near future. The experiments of X-ray crystallography laboratories are agreeing with our theoretical calculations. This article summarized mathematical formulas of prion amyloid fibril cross-β structures of all the above PrP segments currently listed in the Protein Data Bank.
PDFShare this article
Medicinal Chemistry received 6627 citations as per Google Scholar report
