1fkc
From Proteopedia
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| - | [[Image:1fkc.gif|left|200px]] | + | [[Image:1fkc.gif|left|200px]] |
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| - | '''HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231''' | + | {{Structure |
| + | |PDB= 1fkc |SIZE=350|CAPTION= <scene name='initialview01'>1fkc</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FKC is a [ | + | 1FKC 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=1FKC OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases., Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sonnichsen FD, J Biol Chem. 2000 Oct 27;275(43):33650-4. PMID:[http:// | + | Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases., Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sonnichsen FD, J Biol Chem. 2000 Oct 27;275(43):33650-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10954699 10954699] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: three helix]] | [[Category: three helix]] | ||
| - | ''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 11:10:17 2008'' |
Revision as of 09:10, 20 March 2008
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HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231
Contents |
Overview
Prion propagation in transmissible spongiform encephalopathies involves the conversion of cellular prion protein, PrP(C), into a pathogenic conformer, PrP(Sc). Hereditary forms of the disease are linked to specific mutations in the gene coding for the prion protein. To gain insight into the molecular basis of these disorders, the solution structure of the familial Creutzfeldt-Jakob disease-related E200K variant of human prion protein was determined by multi-dimensional nuclear magnetic resonance spectroscopy. Remarkably, apart from minor differences in flexible regions, the backbone tertiary structure of the E200K variant is nearly identical to that reported for the wild-type human prion protein. The only major consequence of the mutation is the perturbation of surface electrostatic potential. The present structural data strongly suggest that protein surface defects leading to abnormalities in the interaction of prion protein with auxiliary proteins/chaperones or cellular membranes should be considered key determinants of a spontaneous PrP(C) --> PrP(Sc) conversion in the E200K form of hereditary prion disease.
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
1FKC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases., Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sonnichsen FD, J Biol Chem. 2000 Oct 27;275(43):33650-4. PMID:10954699
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