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Crystal structures reveal phosphorylation-dependent disruption of the heat shock protein 70-CHIP interface: A compensatory G132N variant restores binding affinity.
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ID: paper-41833837
📄 Paper Details
Crystal structures reveal phosphorylation-dependent disruption of the heat shock protein 70-CHIP interface: A compensatory G132N variant restores binding affinity.
Stewart M, Paththamperuma C, McCann C, Cottingim K, Zhang H, DelVecchio R, Peng I, Fennimore E, Nix JC, Saeed MN, George K, Makaroff K, Colie M, Paulakonis E, Almeida MF, Afolayan AJ, Brown NG, Page R
Abstract
Heat shock protein 70 (HSP70) and its E3 ligase co-chaperone CHIP (STUB1) form a critical quality-control complex that directs client proteins toward folding or degradation. Phosphorylation of HSP70 at a conserved threonine in the C-terminal tail influences the fate of clients during cellular stress, yet the structural basis for this regulation remains unclear. Here, we present crystal structures of the CHIP tetratricopeptide repeat (TPR) domain bound to unphosphorylated and phosphorylated HSP70...
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