A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
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DOI：
10.1006/jmbi.1997.1328
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发表时间：
1997-10-31
影响因子：
5.6
通讯作者：
Burton, DR
中科院分区：
文献类型：
--
作者：
Peretz, D;Williamson, RA;Burton, DR
痒病朊病毒蛋白 (PrPSc) 是由细胞亚型 (PrPC) 通过涉及深刻构象变化的翻译后过程形成的。使用 ELISA 和免疫沉淀法鉴定 PrPC 和 PrPSc 的蛋白酶抗性核心（指定为 PrP 27-30）上重组抗体 Fab 片段 (Fab) 的线性表位。 PrPC 和 PrP 27-30 中 C 末端的表位区域均可接近；相反，在 PrPC 中可以接近 N 末端区域（残基 90 至 120）的表位，但在 PrP 27-30 中很大程度上是隐秘的。 PrP 27-30 的变性暴露了 N 末端结构域的表位。我们的研究结果表明，PrPSc 形成的主要构象变化发生在 PrP 27-30 的 N 端片段内。 (C) 1997 学术出版社有限公司。
The scrapie prion protein (PrPSc) is formed from the cellular isoform (PrPC) by a post-translational process that involves a profound conformational change. Linear epitopes for recombinant antibody Fab fragments (Fabs) on PrPC and on the protease-resistant core of PrPSc, designated PrP 27-30, were identified using ELISA and immunoprecipitation. An epitope region at the C terminus was accessible in both PrPC and PrP 27-30; in contrast, epitopes towards the N-terminal region (residues 90 to 120) were accessible in PrPC but largely cryptic in PrP 27-30. Denatruation of PrP 27-30 exposed the epitopes of the N-terminal domain. We argue from our findings that the major conformational change underlying PrPSc formation occurs within the N-terminal segment of PrP 27-30. (C) 1997 Academic Press Limited.