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2015 ; 9
(3
): 190-9
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Structure-based view on PSI(+) prion properties
#MMPMID26030475
Bondarev SA
; Zhouravleva GA
; Belousov MV
; Kajava AV
Prion
2015[]; 9
(3
): 190-9
PMID26030475
show ga
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 ?-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 understanding of prion [PSI(+)] stability and propagation.
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