Artikel ; Online: Tertiary structure and conformational dynamics of the anti-amyloidogenic chaperone DNAJB6b at atomistic resolution.
2024 Band 15, Heft 1, Seite(n) 3285
Abstract: DNAJB6b is a molecular chaperone of the heat shock protein network, shown to play a crucial role in preventing aggregation of several disease-related intrinsically disordered proteins. Using homology modeling and microsecond-long all-atom molecular ... ...
Abstract | DNAJB6b is a molecular chaperone of the heat shock protein network, shown to play a crucial role in preventing aggregation of several disease-related intrinsically disordered proteins. Using homology modeling and microsecond-long all-atom molecular dynamics (MD) simulations, we show that monomeric DNAJB6b is a transiently interconverting protein cycling between three states: a closed state, an open state (both abundant), and a less abundant extended state. Interestingly, the reported regulatory autoinhibitory anchor between helix V in the G/F |
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Mesh-Begriff(e) | Humans ; Molecular Chaperones/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/metabolism ; Molecular Dynamics Simulation ; Molecular Conformation ; Muscular Dystrophies, Limb-Girdle ; HSP40 Heat-Shock Proteins/metabolism |
Chemische Substanzen | Molecular Chaperones ; HSP70 Heat-Shock Proteins ; Heat-Shock Proteins ; HSP40 Heat-Shock Proteins |
Sprache | Englisch |
Erscheinungsdatum | 2024-04-16 |
Erscheinungsland | England |
Dokumenttyp | Journal Article |
ZDB-ID | 2553671-0 |
ISSN | 2041-1723 ; 2041-1723 |
ISSN (online) | 2041-1723 |
ISSN | 2041-1723 |
DOI | 10.1038/s41467-024-46587-z |
Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
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