1skh
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1skh.gif|left|200px]] | + | [[Image:1skh.gif|left|200px]] |
| - | + | ||
| - | '''N-terminal (1-30) of bovine Prion protein''' | + | {{Structure |
| + | |PDB= 1skh |SIZE=350|CAPTION= <scene name='initialview01'>1skh</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''N-terminal (1-30) of bovine Prion protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1SKH is a [ | + | 1SKH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SKH OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15554701 15554701] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 19: | Line 28: | ||
[[Category: coil-helix-coil]] | [[Category: coil-helix-coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:06:04 2008'' |
Revision as of 12:06, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 14:06:04 2008
