MassIVE MSV000079205

Partial Public PXD003513

HDX-MS of CHIP wt and K30A mutant

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Description

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

Contact

Principal Investigators:
(in alphabetical order) 		Kathryn L Ball
Submitting User: vikram

Publications

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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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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