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Title [sv]
Struktur och Funktionsstudier på Amyloida Proteiner samt på Proteiner Involverade i Bakterie-Värdcell Interaktioner
Title [en]
Structure-Function Studies of Amyloid Proteins and Virulence-Associated Proteins
Abstract [en]
Chemical Biology involves the use of chemical compounds to study and manipulate biological systems with the ultimate goal of developing new therapies for diseases. Chemical biologists of relevance for this application include chemists, biochemists, molecular- and cell biologists, and clinicians. In this application we study the crystal structures of interactions of natural or small synthetic compounds with their target biomolecules and analyze how these interactions regulate biochemical pathways within cells and tissues. This concept is applied to two projects: Transthyrein (TTR) - a plasma protein that causes amyloid disease (?Skelleftesjukan?), and PrfA - the master regulator for virulence genes in the human pathogen Listeria monocytogenes. PrfA belongs to the Crp/Fnr family of regulators with over 1200 protein members including members in other important Gram-positive and Gram-negative bacteria causing serious disease in humans. Other projects which are part of this application include studies of proteins involved in bacteria-host cell interactions. Proteins of interest include the metalloprotease PrtV from Vibrio cholera, and the regulatory transcription factor CpxR from Yersinia pseudotuberculosis. For these and other studies, we routinely complement our crystallographic methods with a number of other biophysical and biochemical methods.
Principal InvestigatorSauer-Eriksson, Elisabeth
Coordinating organisation
Umeå University
Funder
Period
2016-01-01 － 2018-12-31
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
DiVA, id: project:1446Project, id: 2015-03607_VR
v. 2.43.0
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