This title appears in the Scientific Report :
2008
Please use the identifier:
http://dx.doi.org/10.1073/pnas.0804721105 in citations.
Structural changes of membrane-anchored native PrPc
Structural changes of membrane-anchored native PrPc
Misfolding and subsequent aggregation of endogenous proteins constitute essential steps in many human disorders, including Alzheimer and prion diseases. In most prion protein-folding studies, the posttranslational modifications, the lipid anchor in particular, were lacking. Here, we studied a fully...
Saved in:
Personal Name(s): | Elfrink, K. |
---|---|
Ollesch, J. / Stoehr, J. / Willbold, D. / Riesner, D. / Gerwert, K. | |
Contributing Institute: |
Molekulare Biophysik; INB-2 |
Published in: | Proceedings of the National Academy of Sciences of the United States of America, 105 (2008) S. 10815 - 10819 |
Imprint: |
Washington, DC
Academy
2008
|
Physical Description: |
10815 - 10819 |
PubMed ID: |
18669653 |
DOI: |
10.1073/pnas.0804721105 |
Document Type: |
Journal Article |
Research Program: |
Funktion und Dysfunktion des Nervensystems |
Series Title: |
Proceedings of the National Academy of Sciences of the United States of America
105 |
Subject (ZB): | |
Publikationsportal JuSER |
Misfolding and subsequent aggregation of endogenous proteins constitute essential steps in many human disorders, including Alzheimer and prion diseases. In most prion protein-folding studies, the posttranslational modifications, the lipid anchor in particular, were lacking. Here, we studied a fully posttranslationally modified cellular prion protein, carrying two N-glycosylations and the natural GPI anchor. We used time-resolved FTIR to study the prion protein secondary structure changes when binding to a raft-like lipid membrane via its GPI anchor. We observed that membrane anchoring above a threshold concentration induced refolding of the prion protein to intermolecular beta-sheets. Such transition is not observed in solution and is membrane specific. Excessive membrane anchoring, analyzed with molecular sensitivity, is thought to be a crucial event in the development of prion diseases. |