1I4M
Crystal structure of the human prion protein reveals a mechanism for oligomerization
Summary for 1I4M
| Entry DOI | 10.2210/pdb1i4m/pdb |
| Descriptor | MAJOR PRION PROTEIN, CADMIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | domain-swapped dimer, membrane protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156 |
| Total number of polymer chains | 1 |
| Total formula weight | 12975.42 |
| Authors | Knaus, K.J.,Morillas, M.,Swietnicki, W.,Malone, M.,Surewicz, W.K.,Yee, V.C. (deposition date: 2001-02-22, release date: 2002-02-27, Last modification date: 2024-11-13) |
| Primary citation | Knaus, K.J.,Morillas, M.,Swietnicki, W.,Malone, M.,Surewicz, W.K.,Yee, V.C. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat.Struct.Biol., 8:770-774, 2001 Cited by PubMed Abstract: The pathogenesis of transmissible encephalopathies is associated with the conversion of the cellular prion protein, PrP(C), into a conformationally altered oligomeric form, PrP(Sc). Here we report the crystal structure of the human prion protein in dimer form at 2 A resolution. The dimer results from the three-dimensional swapping of the C-terminal helix 3 and rearrangement of the disulfide bond. An interchain two-stranded antiparallel beta-sheet is formed at the dimer interface by residues that are located in helix 2 in the monomeric NMR structures. Familial prion disease mutations map to the regions directly involved in helix swapping. This crystal structure suggests that oligomerization through 3D domain-swapping may constitute an important step on the pathway of the PrP(C) --> PrP(Sc) conversion. PubMed: 11524679DOI: 10.1038/nsb0901-770 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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