1M25
STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE IN TFE SOLUTION
Summary for 1M25
| Entry DOI | 10.2210/pdb1m25/pdb |
| Related | 1G04 |
| NMR Information | BMRB: 5405 |
| Descriptor | MAJOR PRION PROTEIN (1 entity in total) |
| Functional Keywords | helix, prion, tfe, unknown function |
| Cellular location | Cell membrane; Lipid-anchor, GPI-anchor: P23907 |
| Total number of polymer chains | 1 |
| Total formula weight | 3431.73 |
| Authors | Megy, S.,Bertho, G.,Kozin, S.A.,Coadou, G.,Debey, P.,Hoa, G.H.,Girault, J.-P. (deposition date: 2002-06-21, release date: 2002-07-17, Last modification date: 2024-05-22) |
| Primary citation | Megy, S.,Bertho, G.,Kozin, S.A.,Debey, P.,Hoa, G.H.,Girault, J.-P. Possible role of region 152-156 in the structural duality of a peptide fragment from sheep prion protein Protein Sci., 13:3151-3160, 2004 Cited by PubMed Abstract: The conformational conversion of the nonpathogenic "cellular" prion isoform into a pathogenic "scrapie" protease-resistant isoform is a fundamental event in the onset of transmissible spongiform encephalopathies (TSE). During this pathogenic conversion, helix H1 and its two flanking loops of the normal prion protein are thought to undergo a conformational transition into a beta-like structure. A peptide spanning helix H1 and beta-strand S2 (residues 142-166 in human numbering) was studied by circular dichroism and nuclear magnetic resonance spectroscopies. This peptide in aqueous solution, in contrast to many prion fragments studied earlier (1) is highly soluble and (2) does not aggregate until the millimolar concentration range, and (3) exhibits an intrinsic propensity to a beta-hairpin-like conformation at neutral pH. We found that this peptide can also fold into a helix H1 conformation when dissolved in a TFE/PB mixture. The structures of the peptide calculated by MD showed solvent-dependent internal stabilizing forces of the structures and evidenced a higher mobility of the residues following the end of helix H1. These data suggest that the molecular rearrangement of this peptide in region 152-156, particularly in position 155, could be associated with the pathogenic conversion of the prion protein. PubMed: 15537751DOI: 10.1110/ps.04745004 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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