4E1I

Fragment of human prion protein

Summary for 4E1I

• Entry DOI: 10.2210/pdb4e1i/pdb
• Related: 4E1H
• Descriptor: Major prion protein (3 entities in total)
• Functional Keywords: beta prism, amyloid-related oligomer, protein fibril, cell cycle
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156 P04156
• Total number of polymer chains: 12
• Total formula weight: 8547.85

Authors

Apostol, M.I.,Surewicz, W.K. (deposition date: 2012-03-06, release date: 2013-03-06, Last modification date: 2013-11-27)

Primary citation

Apostol, M.I.,Perry, K.,Surewicz, W.K.
Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.
J.Am.Chem.Soc., 135:10202-10205, 2013

PubMed Abstract: 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 before observed structural motif for ordered protein aggregates and suggests a possible mechanism for self-propagation of misfolded conformations by such nonamyloid oligomers.

PubMed: 23808589
DOI: 10.1021/ja403001q

Experimental method

X-RAY DIFFRACTION (2.03 Å)