Conformational Change and Assembly through Edge Strands in Transthyretin and Other Amyloid Proteins

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• 作者：Janel Laidman ; G. Jason Forse ; Todd O. Yeates
• 刊名：Accounts of Chemical Research
• 出版年：2006
• 出版时间：September 2006
• 年：2006
• 卷：39
• 期：9
• 页码：576 - 583
• 全文大小：383K
• 年卷期：v.39,no.9(September 2006)
• ISSN：1520-4898

文摘

Numerous diseases are characterized by the formation of insoluble,amyloid protein fibrils. Intensive investigations are beginning tounravel the detailed molecular and structural principles thatunderlie the spontaneous formation of these fibrils. The amyloidprotein transthyretin serves as an excellent system for dissectingthe conformational changes and ensuing subunit-subunit associations that lead to amyloid. One working model for tranthyretinamyloid involves the exposure of an "unprotected" edge ges/gifchars/beta2.gif" BORDER=0 ALIGN="middle"> strand,followed by symmetric assembly of subunits to give head-to-headand tail-to-tail protofibrils. The models and principles emergingfrom studies on transthyretin lead to connections to other amyloidsystems.