Abstract 2639 Structural analysis of the glycine-rich region and its role in J-domain protein interaction with molecular chaperone Hsp70

Numerous human neurodegenerative disorders, such as Alzheimer's, Parkinson's, or Huntington's diseases, are considered protein-misfolding diseases. In all these cases, disease-specific proteins aggregate in a highly organized manner, forming large insoluble amyloid-like fibrils. The natural defense of the cell against protein misfolding and aggregation is a network of molecular chaperones, with the central role of Hsp70s and their obligatory J-domain protein (JDP) partners. In the current model, a versatile activity of Hsp70 is targeted towards specific processes by a cohort of diverse JDP cochaperones, with the most abundant representing class A and B (DNAJA1 and DNAJB1 in humans).