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Title [sv]
Strukturella studier på amyloida proteiner samt på proteiner involverade i bakterie-värdcell interaktioner
Title [en]
Exploring mechanisms for amyloid formation and for bacteria-host cell interactions.
Abstract [sv]
The human plasma protein transthyretin (TTR) is normally a soluble protein that functions as transport protein for thyroxin. However, point-mutations in the human protein lead to structural changes and cause familial amyloidotic polyneuropathy (FAP, type I, Skelleftesjukan). The aim of our work is to characterize in detail the structural changes in the TTR protein that lead to amyloid formation and disease. This information is valuable for the design of drugs that prevent the TTR protein from self-assembly. Using predominantly X-ray crystallographic techniques, we study the structure of the normal native form of TTR, the structures of altered TTR proteins that carry mutations known to cause disease, and TTR from other species. In other projects we also perform structure-function studies of proteins and protein complexes involved in bacteria host-cell interactions. Proteins of interest include metalloproteases from Vibrio cholera and protein components from type III secretion system from Yersinia pseudotuberculosis.
Principal InvestigatorSauer-Eriksson, Elisabeth
Coordinating organisation
Umeå University
Funder
Period
2010-01-01 － 2012-12-31
Identifiers
DiVA, id: project:931Project, id: 2009-03708_VR

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