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1i4m
From Proteopedia
(New page: 200px<br /> <applet load="1i4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i4m, resolution 2.00Å" /> '''Crystal structure o...) |
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| - | [[Image:1i4m.gif|left|200px]]<br /> | + | [[Image:1i4m.gif|left|200px]]<br /><applet load="1i4m" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1i4m" size=" | + | |
caption="1i4m, resolution 2.00Å" /> | caption="1i4m, resolution 2.00Å" /> | ||
'''Crystal structure of the human prion protein reveals a mechanism for oligomerization'''<br /> | '''Crystal structure of the human prion protein reveals a mechanism for oligomerization'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The pathogenesis of transmissible encephalopathies is associated with the | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CD and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1I4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Knaus, K | + | [[Category: Knaus, K J.]] |
[[Category: Malone, M.]] | [[Category: Malone, M.]] | ||
[[Category: Morillas, M.]] | [[Category: Morillas, M.]] | ||
| - | [[Category: Surewicz, W | + | [[Category: Surewicz, W K.]] |
[[Category: Swietnicki, W.]] | [[Category: Swietnicki, W.]] | ||
| - | [[Category: Yee, V | + | [[Category: Yee, V C.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: domain-swapped dimer]] | [[Category: domain-swapped dimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:58 2008'' |
Revision as of 11:07, 21 February 2008
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Crystal structure of the human prion protein reveals a mechanism for oligomerization
Contents |
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 and 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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