1g04
From Proteopedia
(New page: 200px<br /><applet load="1g04" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g04" /> '''SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTI...) |
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| - | [[Image:1g04.gif|left|200px]]<br /><applet load="1g04" size=" | + | [[Image:1g04.gif|left|200px]]<br /><applet load="1g04" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g04" /> | caption="1g04" /> | ||
'''SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE'''<br /> | '''SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | According to the "protein only" hypothesis, a conformational conversion of | + | According to the "protein only" hypothesis, a conformational conversion of the non-pathogenic "cellular" prion isoform into a pathogenic "scrapie" isoform is the fundamental event in the onset of prion diseases. During this pathogenic conversion, helix H1 and two adjacent surface loops L2 and L3 of the normal prion protein are thought to undergo a conformational transition into an extended beta-like structure, which is prompted by interactions with the pre-existing beta-sheet. To get more insight into the interaction between the helix and one of the beta-strands in the partially unfolded prion protein, the solution structure of a synthetic linear peptide spanning helix H1 and beta-strand S2 (residues 142-166 in human numbering) was studied by circular dichroism and nuclear magnetic resonance spectroscopies. We found that, in contrast to many prion fragments studied earlier, this peptide (i) is highly soluble and does not aggregate up to a millimolar concentration range in aqueous medium and (ii) exhibits an intrinsic propensity to a beta-hairpin like conformation at neutral pH. This beta-propensity can be one of the internal driving forces of the molecular rearrangement responsible for the pathogenic conversion of the prion protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1G04 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1G04 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G04 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bertho, G.]] | [[Category: Bertho, G.]] | ||
[[Category: Debey, P.]] | [[Category: Debey, P.]] | ||
| - | [[Category: Girault, J | + | [[Category: Girault, J P.]] |
[[Category: Haertle, T.]] | [[Category: Haertle, T.]] | ||
| - | [[Category: Hoa, G | + | [[Category: Hoa, G Hui Bon.]] |
| - | [[Category: Kozin, S | + | [[Category: Kozin, S A.]] |
| - | [[Category: Mazur, A | + | [[Category: Mazur, A K.]] |
[[Category: Rabesona, H.]] | [[Category: Rabesona, H.]] | ||
[[Category: Takahashi, M.]] | [[Category: Takahashi, M.]] | ||
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[[Category: prion]] | [[Category: prion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:31 2008'' |
Revision as of 10:44, 21 February 2008
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SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE
Overview
According to the "protein only" hypothesis, a conformational conversion of the non-pathogenic "cellular" prion isoform into a pathogenic "scrapie" isoform is the fundamental event in the onset of prion diseases. During this pathogenic conversion, helix H1 and two adjacent surface loops L2 and L3 of the normal prion protein are thought to undergo a conformational transition into an extended beta-like structure, which is prompted by interactions with the pre-existing beta-sheet. To get more insight into the interaction between the helix and one of the beta-strands in the partially unfolded prion protein, the solution structure of a synthetic linear peptide spanning helix H1 and beta-strand S2 (residues 142-166 in human numbering) was studied by circular dichroism and nuclear magnetic resonance spectroscopies. We found that, in contrast to many prion fragments studied earlier, this peptide (i) is highly soluble and does not aggregate up to a millimolar concentration range in aqueous medium and (ii) exhibits an intrinsic propensity to a beta-hairpin like conformation at neutral pH. This beta-propensity can be one of the internal driving forces of the molecular rearrangement responsible for the pathogenic conversion of the prion protein.
About this Structure
1G04 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution., Kozin SA, Bertho G, Mazur AK, Rabesona H, Girault JP, Haertle T, Takahashi M, Debey P, Hoa GH, J Biol Chem. 2001 Dec 7;276(49):46364-70. Epub 2001 Sep 27. PMID:11577109
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