Journal
EMBO JOURNAL
Volume 20, Issue 7, Pages 1547-1554Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.7.1547
Keywords
conformational change; phage display; prion protein; recombinant antibodies
Categories
Funding
- NHLBI NIH HHS [HL63817] Funding Source: Medline
- NIA NIH HHS [P01 AG002132, AG02132] Funding Source: Medline
- NINDS NIH HHS [NS14069] Funding Source: Medline
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It is hypothesized that infectious prions are generated as the cellular form of the prion protein (PrPC) undergoes pronounced conformational change under the direction of an infectious PrPSc template. Conversion to the infectious conformer is particularly associated with major structural rearrangement in the central portion of the protein (residues 90-120), which has an extended flexible structure in the PrPC isoform. Using a panel of recombinant antibodies reactive with different parts of PrP, we show that equivalent major structural rearrangements occur spontaneously in this region of PrP immobilized on a surface. In contrast, regions more towards the termini of the protein remain relatively unaltered. The rearrangements occur even under conditions where individual PrP molecules should not contact one another. The propensity of specific unstructured regions of PrP to spontaneously undergo large and potentially deleterious conformational changes may have important implications for prion biology.
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