1i4m

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[[Image:1i4m.gif|left|200px]]
[[Image:1i4m.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1i4m", creates the "Structure Box" on the page.
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{{STRUCTURE_1i4m| PDB=1i4m | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4m OCA], [http://www.ebi.ac.uk/pdbsum/1i4m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i4m RCSB]</span>
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'''Crystal structure of the human prion protein reveals a mechanism for oligomerization'''
'''Crystal structure of the human prion protein reveals a mechanism for oligomerization'''
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[[Category: Swietnicki, W.]]
[[Category: Swietnicki, W.]]
[[Category: Yee, V C.]]
[[Category: Yee, V C.]]
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[[Category: domain-swapped dimer]]
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[[Category: Domain-swapped dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:34:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:33 2008''
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Revision as of 16:34, 2 May 2008

Template:STRUCTURE 1i4m

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


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.

About this Structure

1I4M is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Fri May 2 19:34:00 2008

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