HDX-MS was used to establish that conformational-inhibition-signals extended from the TPR-domain to the U-box of CHIP. This underscores inter-domain allosteric regulation of CHIP by the core molecular chaperones. Defining the chaperone-associated TPR-domain of CHIP as a manager of inter-domain communication highlights the potential for scaffolding modules to regulate, as well as assemble, complexes that are fundamental to protein homeostatic control.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: HDX-MS ; Allostery ; Ubiquitination ; E3-ligase ; TPR-domain ; Cochaperones
Principal Investigators: (in alphabetical order) |
Kathryn L Ball |
Submitting User: | vikram |
Narayan V, Landré V, Ning J, Hernychova L, Muller P, Verma C, Walkinshaw MD, Blackburn EA, Ball KL.
Protein-Protein Interactions Modulate the Docking-Dependent E3-Ubiquitin Ligase Activity of Carboxy-Terminus of Hsc70-Interacting Protein (CHIP).
Mol. Cell Proteomics. 2015 Nov;14(11):2973-87. Epub 2015 Sep 1.
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