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COMPUTATIONAL STUDIES OF PRION PROTEIN STRUCTURE

COMPUTATIONAL STUDIES OF PRION PROTEIN STRUCTURE
朊病毒蛋白结构的计算研究
批准号：
6097930
负责人：
FRED E COHEN
金额：
$22.21万
依托单位：
UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
依托单位国家：
美国
项目类别：
财政年份：
1999
资助国家：
美国
项目状态：
已结题
起止时间：
1999-06-01 至 1999-12-31
来源：
https://reporter.nih.gov/project-details/6097930
关键词：
chemical models computer simulation conformation molecular dynamics nucleic acid repetitive sequence prions protein folding protein isoforms protein sequence protein structure scrapie site directed mutagenesis thermodynamics

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中文摘要
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英文摘要
Prion diseases are diseases of protein conformation where the folding of PrP displays non Anfinsenian behavior. We wish to understand the energy landscape that PrP must confront as it folds to form PrPC under normal physiological conditions and how it can refold to form aberrant pathologic conditions. In this project, we will use lattice models of proteins to explore the general features of sequences that allow prion-like behavior instead of more classical Anfinsenian folding. We will study the relevance of these ideas to the mechanisms for inherited disease. Finally, while we now he a better understanding of the three dimensional structure of PrPC from residues 125-231, we still do not know much about the structure of the holoprotein including the octarepeat region (23-90) complexed to copper. Our insight into the structure of PrPSc is even more limited. However, we believe that we can leverage our results on the PrPSc 106 mini prion to learn more about the structural constraints on PrPSc.
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会议论文
UNDERSTANDING AND IMPROVING SMALL MOLECULE INHIBITORS OF PRION REPLICATION
STRUCTURE BASED DESIGN OF ANTI PRION THERAPEUTICS
TOWARD A STRUCTURE OF PrPSc
STRUCTURE BASED DESIGN OF ANTI PRION THERAPEUTICS
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