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Structures and Activities of Prions and Prion Proteins

Structures and Activities of Prions and Prion Proteins
朊病毒和朊病毒蛋白的结构和活性
批准号：
10014041
负责人：
BYRON CAUGHEY
金额：
$17.55万
依托单位：
NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES
依托单位国家：
美国
项目类别：
财政年份：
--
资助国家：
美国
项目状态：
未结题
起止时间：
至
来源：
https://reporter.nih.gov/project-details/10014041
关键词：
AmyloidAmyloid FibrilsAmyloid ProteinsBovine Spongiform EncephalopathyBrainChronic Wasting DiseaseCreutzfeldt-Jakob SyndromeCryoelectron MicroscopyDiseaseGoalsLateralMolecularNeurodegenerative DisordersPathogenesisPathologicPrPPrPSc ProteinsPrion DiseasesResolutionRunningScrapieStructureVertebral columnbasebeta pleated sheetdisease transmissionimage reconstructionsynucleintau Proteinstransmission process

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中文摘要
翻译
感染形式的朊病毒蛋白PrPSc的结构尚不清楚。最近解决蛋白淀粉样蛋白原纤维结构的一种方法是冷冻电子显微镜，最近被其他研究小组用于揭示与疾病相关的tau和突触核蛋白原纤维的淀粉样蛋白核心结构。我们已经开始追求基于低温电子显微镜的PrPSc结构解析。已经取得了进展，横向视图和图像重建显示堆叠的β片垂直于原纤维轴。板材之间的间距为4.8 A。然而，到目前为止，获得的分辨率还不足以破译脑源性PrPSc淀粉样蛋白原纤维核心的骨干折叠。
英文摘要
The structure of the infectious form of prion protein, PrPSc, remains unclear. One recent approach to solving protein amyloid fibril structures is cryo-electron microscopy, which has recently been used by other groups to reveal the amyloid core structures of disease-associated tau and synuclein fibrils. We have begun to pursue cryo-electron microscopy-based elucidation of PrPSc structure. Progress has been made, with lateral views and image reconstructions revealing stacked beta sheets running perpendicular to the fibril axis. The spacing between the sheets is 4.8 A. However, so far the resolution obtained has been insufficient to decipher the backbone folding of the core of amyloid fibrils of brain-derived PrPSc.
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会议论文
Prion Disease Therapeutics
Structures and Activities of Prions and Prion Proteins
Prion Disease Therapeutics
Detection of Prions
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