Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae

被引：109

作者：

Bousset, L

Belrhali, H

Janin, J

Melki, R

Morera, S

机构：

[1] CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France

[2] European Synchrotron Radiat Facil, F-38043 Grenoble, France

来源：

STRUCTURE | 2001年 / 9卷 / 01期

关键词：

D O I：

10.1016/S0969-2126(00)00553-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Background: The [URE3] non-Mendelian element of the yeast S. cerevisiae is due to the propagation of a transmissible form of the protein Ure2. The infectivity of Ure2p is thought to originate from a conformational change of the normal form of the prion protein. This conformational change generates a form of Ure2p that assembles into amyloid fibrils. Hence, knowledge of the three-dimensional structure of prion proteins such as Ure2p should help in understanding the mechanism of amyloid formation associated with a number of neurodegenerative diseases.

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页码：39 / 46

页数：8

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