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SHR Neuro Krebs Kardio Lipid Stoffw Microb

Alderson, TR; Kim, JH; Markley, JL.
Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.
Structure. 2016; 24(7): 1014-30. Doi: 10.1016/j.str.2016.05.011 [OPEN ACCESS]
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Führende Autor*innen der Med Uni Graz
Alderson Thomas Reid

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Protein misfolding and aggregation are pathological events that place a significant amount of stress on the maintenance of protein homeostasis (proteostasis). For prevention and repair of protein misfolding and aggregation, cells are equipped with robust mechanisms that mainly rely on molecular chaperones. Two classes of molecular chaperones, heat shock protein 70 kDa (Hsp70) and Hsp40, recognize and bind to misfolded proteins, preventing their toxic biomolecular aggregation and enabling refolding or targeted degradation. Here, we review the current state of structural biology of Hsp70 and Hsp40-Hsp70 complexes and examine the link between their structures, dynamics, and functions. We highlight the power of nuclear magnetic resonance spectroscopy to untangle complex relationships behind molecular chaperones and their mechanism(s) of action.
Find related publications in this database (using NLM MeSH Indexing)
Animals - administration & dosage
HSP40 Heat-Shock Proteins - chemistry, metabolism
HSP70 Heat-Shock Proteins - chemistry, metabolism
Humans - administration & dosage
Molecular Dynamics Simulation - administration & dosage
Protein Folding - administration & dosage

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