4E1H: Fragment of human prion protein

The structural transition of the prion protein from alpha-helical- to beta-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 beta-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.
PDB ID: 4E1HDownload
MMDB ID: 108129
PDB Deposition Date: 2012/3/6
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.4  Å
Similar Structures:
Biological Unit for 4E1H: dodecameric; determined by author and by software (PISA)
Molecular Components in 4E1H
Label Count Molecule
Proteins (12 molecules)
Major Prion Protein(Gene symbol: PRNP)
Molecule annotation
Major Prion Protein(Gene symbol: PRNP)
Molecule annotation
Chemicals (7 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB