1i4m
From Proteopedia
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| - | [[Image:1i4m.gif|left|200px]] | + | [[Image:1i4m.gif|left|200px]] |
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| - | '''Crystal structure of the human prion protein reveals a mechanism for oligomerization''' | + | {{Structure |
| + | |PDB= 1i4m |SIZE=350|CAPTION= <scene name='initialview01'>1i4m</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the human prion protein reveals a mechanism for oligomerization''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I4M is a [ | + | 1I4M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4M OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11524679 11524679] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: domain-swapped dimer]] | [[Category: domain-swapped dimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:45:29 2008'' |
Revision as of 09:45, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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