Unknown

Dataset Information

0

Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.

ABSTRACT: The structural transition of the prion protein from ?-helical- to ?-sheet-rich underlies its conversion into infectious and disease-associated isoforms. Here we describe the crystal structure of a fragment from human prion protein consisting of the disulfide-bond-linked portions of helices 2 and 3. Instead of forming a pair-of-sheets steric zipper structure characteristic of amyloid fibers, this fragment crystallized into a ?-sheet-rich assembly of hexameric oligomers. This study reveals a never before observed structural motif for ordered protein aggregates and suggests a possible mechanism for self-propagation of misfolded conformations by such nonamyloid oligomers.

SUBMITTER: Apostol MI 

PROVIDER: S-EPMC3766960 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.

Apostol Marcin I MI   Perry Kay K   Surewicz Witold K WK  

Journal of the American Chemical Society 20130702 28

The structural transition of the prion protein from α-helical- to β-sheet-rich underlies its conversion into infectious and disease-associated isoforms. Here we describe the crystal structure of a fragment from human prion protein consisting of the disulfide-bond-linked portions of helices 2 and 3. Instead of forming a pair-of-sheets steric zipper structure characteristic of amyloid fibers, this fragment crystallized into a β-sheet-rich assembly of hexameric oligomers. This study reveals a never  ...[more]

Similar Datasets

Unknown Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in Alzheimer's disease.
| S-EPMC6623621 | biostudies-literature
Unknown The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p.
| S-EPMC29279 | biostudies-literature
Unknown Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.
| S-EPMC6492631 | biostudies-literature
Unknown Crystal structure of human prion protein bound to a therapeutic antibody.
| S-EPMC2637903 | biostudies-literature
Unknown Unique Properties of the Rabbit Prion Protein Oligomer.
| S-EPMC4987043 | biostudies-literature
Unknown A variational model for oligomer-formation process of GNNQQNY peptide from yeast prion protein Sup35.
| S-EPMC3274832 | biostudies-other
Unknown The crystal structure of an octapeptide repeat of the prion protein in complex with a Fab fragment of the POM2 antibody.
| S-EPMC3719084 | biostudies-literature
Unknown Crystal structure of human Acinus RNA recognition motif domain.
| S-EPMC6057467 | biostudies-literature
Unknown Accumulation of cellular prion protein within β-amyloid oligomer plaques in aged human brains.
| S-EPMC8412093 | biostudies-literature
Unknown The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1.
| S-EPMC2254625 | biostudies-literature