1skh
From Proteopedia
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N-terminal (1-30) of bovine Prion protein
Overview
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.
About this Structure
1SKH is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein., Biverstahl H, Andersson A, Graslund A, Maler L, Biochemistry. 2004 Nov 30;43(47):14940-7. PMID:15554701
Page seeded by OCA on Wed Nov 21 02:26:19 2007
