| Abstract | Molecular Chaperones play an important role in the maintenance of cellular proteins by
carrying out functions ranging from folding newly synthesized proteins to refolding stress
induced aggregated proteins. An accumulation of aggregated proteins is linked to human disease like Alzheimer’s disease (AD), this is one of the main leading causes of death in the United States and it results in severe symptoms such as memory loss and brain
disfunction. A hallmark of this disease is the abundance of structurally abnormal proteins,
which are thought to be a factor of neuronal cell death. These proteins aggregate in an
organized matter forming fibrils which can be defragmented only by activity of molecular chaperone DNAJB1. DNAJB1 is an obligatory partner of HSP70, and it is composed of different domains including the dimerization domain (DD). My research is focusing on how the dimer is formed and its function. To explore the DD, I first investigated the available structure information to identify molecular interactions allowing for the homodimer
formation. Our next goal is to introduce asymmetry into the structure to be able to control the dimerization process. This research aims to dissect the DD as well as test the biological relevance of the dimerization process. We hope that this effort will provide new insights into how DNAJB1 enables the propagation of Alzheimer’s disease.
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