1oeh
From Proteopedia
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| - | [[Image:1oeh.jpg|left|200px]] | + | [[Image:1oeh.jpg|left|200px]] |
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| - | '''HUMAN PRION PROTEIN 61-68''' | + | {{Structure |
| + | |PDB= 1oeh |SIZE=350|CAPTION= <scene name='initialview01'>1oeh</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN PRION PROTEIN 61-68''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OEH is a [ | + | 1OEH 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=1OEH OCA]. |
==Reference== | ==Reference== | ||
| - | The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site., Zahn R, J Mol Biol. 2003 Nov 28;334(3):477-88. PMID:[http:// | + | The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site., Zahn R, J Mol Biol. 2003 Nov 28;334(3):477-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14623188 14623188] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: disease mutation]] | [[Category: disease mutation]] | ||
[[Category: nmr structure]] | [[Category: nmr structure]] | ||
| - | [[Category: octapeptide | + | [[Category: octapeptide repeat]] |
[[Category: ph-dependent conformation]] | [[Category: ph-dependent conformation]] | ||
[[Category: prion protein]] | [[Category: prion protein]] | ||
[[Category: protein aggregation]] | [[Category: protein aggregation]] | ||
| - | ''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 13:09:44 2008'' |
Revision as of 11:09, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN PRION PROTEIN 61-68
Contents |
Overview
Structural studies of mammalian prion protein at pH values between 4.5 and 5.5 established that the N-terminal 100 residue domain is flexibly disordered. Here, we show that at pH values between 6.5 and 7.8, i.e. the pH at the cell membrane, the octapeptide repeats in recombinant human prion protein hPrP(23-230) encompassing the highly conserved amino acid sequence PHGGGWGQ are structured. The nuclear magnetic resonance solution structure of the octapeptide repeats at pH 6.2 reveals a new structural motif that causes a reversible pH-dependent PrP oligomerization. Within the aggregation motif the segments HGGGW and GWGQ adopt a loop conformation and a beta-turn-like structure, respectively. Comparison with the crystal structure of HGGGW-Cu(2+) indicates that the binding of copper ions induces a conformational transition that presumably modulates PrP aggregation. The knowledge that the cellular prion protein is immobilized on the cell surface along with our results suggests a functional role of aggregation in endocytosis or homophilic cell adhesion.
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
1OEH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site., Zahn R, J Mol Biol. 2003 Nov 28;334(3):477-88. PMID:14623188
Page seeded by OCA on Thu Mar 20 13:09:44 2008
