1HJN
HUMAN PRION PROTEIN AT PH 7.0
Summary for 1HJN
| Entry DOI | 10.2210/pdb1hjn/pdb |
| Related | 1E1G 1E1J 1E1P 1E1S 1E1U 1E1W 1HJM |
| Descriptor | MAJOR PRION PROTEIN PRECURSOR (1 entity in total) |
| Functional Keywords | prion protein, prion, brain, glycoprotein, gpi-anchor |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156 |
| Total number of polymer chains | 1 |
| Total formula weight | 12559.97 |
| Authors | Calzolai, L.,Zahn, R. (deposition date: 2003-02-27, release date: 2003-07-03, Last modification date: 2024-11-13) |
| Primary citation | Calzolai, L.,Zahn, R. Influence of Ph on NMR Structure and Stability of the Human Prion Protein Globular Domain J.Biol.Chem., 278:35592-, 2003 Cited by PubMed Abstract: The NMR structure of the globular domain of the human prion protein (hPrP) with residues 121-230 at pH 7.0 shows the same global fold as the previously published structure determined at pH 4.5. It contains three alpha-helices, comprising residues 144-156, 174-194, and 200-228, and a short anti-parallel beta-sheet, comprising residues 128-131 and 161-164. There are slight, strictly localized, conformational changes at neutral pH when compared with acidic solution conditions: helix alpha1 is elongated at the C-terminal end with residues 153-156 forming a 310-helix, and the population of helical structure in the C-terminal two turns of helix alpha 2 is increased. The protonation of His155 and His187 presumably contributes to these structural changes. Thermal unfolding monitored by far UV CD indicates that hPrP-(121-230) is significantly more stable at neutral pH. Measurements of amide proton protection factors map local differences in protein stability within residues 154-157 at the C-terminal end of helix alpha 1 and residues 161-164 of beta-strand 2. These two segments appear to form a separate domain that at acidic pH has a larger tendency to unfold than the overall protein structure. This domain could provide a "starting point" for pH-induced unfolding and thus may be implicated in endosomic PrPC to PrPSc conformational transition resulting in transmissible spongiform encephalopathies. PubMed: 12826672DOI: 10.1074/JBC.M303005200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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