Proteomics

Dataset Information

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Hydrogen Deuterium Exchange of PDK1

ABSTRACT: This project consisted of three HDX-MS experiments. First, we compared the dimeric PDK1(SKD-PIF) to monomeric PDK1(SKD) and mapped the differences in deuterium incorporation onto the dimer model. We then compared the deuterium incorporation kinetics for the kinase (PDK1(SKD)) and PH (PDK1(PH) domains of PDK1 with full-length PDK1 (PDK1(FL)) in pairwise experiments.

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: John Burke

PROVIDER: PXD027401 | Pride | 2022-05-20

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
08_01_20_BMHDX5_Dimer_0.3s_1_0_01_12373.d.zip Other
08_01_20_BMHDX5_Dimer_ND_0_01_12367.d.zip Other
08_01_20_BMHDX5_Mono_0.3s_1_0_01_12371.d.zip Other
08_01_20_BMHDX5_Mono_ND_0_01_12369.d.zip Other
09_01_20_BMHDX5_Dimer_300s_1_0_01_12380.d.zip Other
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Publications

Activation of the essential kinase PDK1 by phosphoinositide-driven trans-autophosphorylation.

Levina Aleksandra A   Fleming Kaelin D KD   Burke John E JE   Leonard Thomas A TA  

Nature communications 20220406 1

3-phosphoinositide-dependent kinase 1 (PDK1) is an essential serine/threonine protein kinase, which plays a crucial role in cell growth and proliferation. It is often referred to as a 'master' kinase due to its ability to activate at least 23 downstream protein kinases implicated in various signaling pathways. In this study, we have elucidated the mechanism of phosphoinositide-driven PDK1 auto-activation. We show that PDK1 trans-autophosphorylation is mediated by a PIP<sub>3</sub>-mediated face-  ...[more]

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