1i4m

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spinqualitylabelsall models 1i4m, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the human prion protein reveals a mechanism for oligomerization

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known diseases associated with this structure: Creutzfeldt-Jakob disease OMIM:[176640], Gerstmann-Straussler disease OMIM:[176640], Huntington disease-like 1 OMIM:[176640], Insomnia, fatal familial OMIM:[176640], Prion disease with protracted course OMIM:[176640], Retinitis pigmentosa-11 OMIM:[606419]

About this Structure

1I4M is a Single protein structure of sequence from Homo sapiens with CD and CL as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human prion protein reveals a mechanism for oligomerization., Knaus KJ, Morillas M, Swietnicki W, Malone M, Surewicz WK, Yee VC, Nat Struct Biol. 2001 Sep;8(9):770-4. PMID:11524679

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