Structure and allosteric effects of low-molecular-weight activators on the protein kinase PDK1 (Q27657237)

8

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Ricardo M Biondi

Ricardo M Biondi

12

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Pedro M. Alzari

Pedro M Alzari

11

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Adriana Stroba

2

Adriana Stroba

0 references

Leila Idrissova

5

Leila Idrissova

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Valerie Hindie

1

Valerie Hindie

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author name string

Hua Zhang

3

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Laura A Lopez-Garcia

4

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Daniel Hirschberg

7

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Thomas J D Jørgensen

9

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Matthias Engel

3,5-Diphenylpent-2-enoic acids as allosteric activators of the protein kinase PDK1: structure-activity relationships and thermodynamic characterization of binding as paradigms for PIF-binding pocket-targeting compounds.

10

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publication date

October 2009

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published in

Nature Chemical Biology

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volume

5

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issue

10

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page(s)

758-64

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cites work

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A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation

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Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation

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Phosphoinositide-dependent protein kinase 1, a sensor of protein conformation

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AGC protein kinase phosphorylation and protein kinase C.

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The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB.

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In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation

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Global, in vivo, and site-specific phosphorylation dynamics in signaling networks

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Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP

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The protein kinase complement of the human genome

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Structural basis of Aurora-A activation by TPX2 at the mitotic spindle

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Mechanism for activation of the growth factor-activated AGC kinases by turn motif phosphorylation

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Allosteric activation of the protein kinase PDK1 with low molecular weight compounds

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The structure of MSK1 reveals a novel autoinhibitory conformation for a dual kinase protein.

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Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions

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Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation

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Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA

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The conformational plasticity of protein kinases

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Refinement of macromolecular structures by the maximum-likelihood method

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Crystal structure of an inactive Akt2 kinase domain

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Automated protein model building combined with iterative structure refinement

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A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1.

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

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High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site

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Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions

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Duplicated dockerin subdomains of Clostridium thermocellum endoglucanase CelD bind to a cohesin domain of the scaffolding protein CipA with distinct thermodynamic parameters and a negative cooperativity

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Crystal structure of the kinase domain of serum and glucocorticoid-regulated kinase 1 in complex with AMP-PNP

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Structural basis for control by phosphorylation

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Protein phosphorylation in signaling--50 years and counting

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The structure of dimeric ROCK I reveals the mechanism for ligand selectivity

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Coot: model-building tools for molecular graphics

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In vivo role of the phosphate groove of PDK1 defined by knockin mutation

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Pushing the boundaries of molecular replacement with maximum likelihood

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Regulation of protein kinases in insulin, growth factor and Wnt signalling

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Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

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Crossref

https://api.crossref.org/works/10.1038%2FNCHEMBIO.208

7 January 2021