1SKH
N-terminal (1-30) of bovine Prion protein
Summary for 1SKH
| Entry DOI | 10.2210/pdb1skh/pdb |
| Descriptor | Major prion protein 2 (1 entity in total) |
| Functional Keywords | coil-helix-coil, unknown function |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 3424.28 |
| Authors | Biverstahl, H.,Andersson, A.,Graslund, A.,Maler, L. (deposition date: 2004-03-05, release date: 2005-03-01, Last modification date: 2024-05-22) |
| Primary citation | Biverstahl, H.,Andersson, A.,Graslund, A.,Maler, L. NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein. Biochemistry, 43:14940-14947, 2004 Cited by PubMed Abstract: The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy revealed that the peptide adopts a largely alpha-helical structure in zwitterionic bicelles as well as in DHPC micelles but has a less degree of alpha-helix structure in partly charged bicelles. The solution structure of bPrPp was determined in DHPC micelles, and an alpha-helix was found between residues Ser8 and Ile21. The residues within the helical region show slow amide hydrogen exchange. Translational diffusion measurements in zwitterionic q = 0.5 bicelles show that the peptide does not induce aggregation of the bicelles. Increased quadrupolar splittings were observed in the outer part of the (2)H spectrum of DMPC in q = 3.5 bicelles, indicating that the peptide induces a certain degree of order in the bilayer. The amide hydrogen exchange and the (2)H NMR results are consistent with a slight positive hydrophobic mismatch and that bPrPp forms a stable helix that inserts in a transmembrane location in the bilayer. The structure of bPrPp and its position in the membrane may be relevant for the understanding of how the N-terminal (1-30) part of the bovine PrP functions as a cell-penetrating peptide. These findings may lead to a better understanding of how the prion protein accumulates at the membrane surface and also how the conversion into the scrapie form is carried out. PubMed: 15554701DOI: 10.1021/bi0485070 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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