1oeh
From Proteopedia
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'''HUMAN PRION PROTEIN 61-68''' | '''HUMAN PRION PROTEIN 61-68''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zahn, R.]] | [[Category: Zahn, R.]] | ||
| - | [[Category: | + | [[Category: Nmr structure]] |
| - | [[Category: | + | [[Category: Octapeptide repeat]] |
| - | [[Category: | + | [[Category: Ph-dependent conformation,brain,disease mutation]] |
| - | [[Category: | + | [[Category: Prion protein]] |
| - | [[Category: | + | [[Category: Protein aggregation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:44:50 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:44, 3 May 2008
HUMAN PRION PROTEIN 61-68
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.
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 Sat May 3 03:44:50 2008
