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Molecular mechanisms for protein-encoded inheritance.

Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D
Nat Struct Mol Biol 16 973-8 (2009)
Related entries: 3fod, 3fpo, 3fr1, 3fth, 3ftl, 3ftr, 3fva, 4np8

Cited: 152 times
EuropePMC logo PMID: 19684598

Abstract

In prion inheritance and transmission, strains are phenotypic variants encoded by protein 'conformations'. However, it is unclear how a protein conformation can be stable enough to endure transmission between cells or organisms. Here we describe new polymorphic crystal structures of segments of prion and other amyloid proteins, which offer two structural mechanisms for the encoding of prion strains. In packing polymorphism, prion strains are encoded by alternative packing arrangements (polymorphs) of beta-sheets formed by the same segment of a protein; in segmental polymorphism, prion strains are encoded by distinct beta-sheets built from different segments of a protein. Both forms of polymorphism can produce enduring conformations capable of encoding strains. These molecular mechanisms for transfer of protein-encoded information into prion strains share features with the familiar mechanism for transfer of nucleic acid-encoded information into microbial strains, including sequence specificity and recognition by noncovalent bonds.

Reviews - 3ftk mentioned but not cited (1)

  1. Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective. Hassan S, White K, Terry C. Biosci Rep 42 BSR20211297 (2022)

Articles - 3ftk mentioned but not cited (4)

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