期刊
EMBO JOURNAL
卷 20, 期 7, 页码 1547-1554出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.7.1547
关键词
conformational change; phage display; prion protein; recombinant antibodies
资金
- NHLBI NIH HHS [HL63817] Funding Source: Medline
- NIA NIH HHS [P01 AG002132, AG02132] Funding Source: Medline
- NINDS NIH HHS [NS14069] Funding Source: Medline
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据