1skh
From Proteopedia
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'''N-terminal (1-30) of bovine Prion protein''' | '''N-terminal (1-30) of bovine Prion protein''' | ||
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[[Category: Graslund, A.]] | [[Category: Graslund, A.]] | ||
[[Category: Maler, L.]] | [[Category: Maler, L.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:48:51 2008'' | |
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Revision as of 05:48, 3 May 2008
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 Sat May 3 08:48:51 2008
