Structure-based view on [PSI+] prion properties

S.A. Bondarev, G.A. Zhouravleva, M.V. Belousov, A.V. Kajava

Результат исследований: Научные публикации в периодических изданияхстатья

9 Цитирования (Scopus)

Аннотация

Yeast [PSI+] prion is one of the most suitable and well characterized system for the investigation of the prion phenomenon. However, until recently, the lack of data on the 3D arrangement of Sup35p prion fibrils hindered progress in this area. The recent arrival in this field of new experimental techniques led to the parallel and in-register superpleated β-structure as a consensus model for Sup35p fibrils. Here, we analyzed the effect of amino acid substitutions of the Sup35 protein through the prism of this structural model. Application of a newly developed computational approach, called ArchCandy, gives us a better understanding of the effect caused by mutations on the fibril forming potential of Sup35 protein. This bioinformatics tool can be used for the design of new mutations with desired modification of prion properties. Thus, we provide examples of how today, having progress toward elucidation of the structural arrangement of Sup35p fibrils, researchers can advance more efficiently to a better understa
Язык оригиналаанглийский
Страницы (с-по)190-199
Число страниц10
ЖурналPrion
Том9
Номер выпуска3
DOI
СостояниеОпубликовано - 2015

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