Proteomics

Dataset Information

0

PKD autoinhibition in trans prevents activation loop autophosphorylation in cis

ABSTRACT: HDX-MS analysis of the kinase domain of PKD1, showing that it forms an inactive dimer

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD033139 | Pride | 2023-02-22

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
01_06_21_MPHDX3_PKD_M_3000s_3_0_01_16537.d.zip Other
01_06_21_MPHDX3_PKD_M_300s_3_0_01_16533.d.zip Other
01_06_21_MPHDX3_PKD_M_30s_3_0_01_16529.d.zip Other
01_06_21_MPHDX3_PKD_WT_3000s_3_0_01_16535.d.zip Other
01_06_21_MPHDX3_PKD_WT_300s_3_0_01_16531.d.zip Other
Items per page:
1 - 5 of 39
altmetric image

Publications

PKD autoinhibition in <i>trans</i> regulates activation loop autophosphorylation in <i>cis</i>.

Reinhardt Ronja R   Hirzel Kai K   Link Gisela G   Eisler Stephan A SA   Hägele Tanja T   Parson Matthew A H MAH   Burke John E JE   Hausser Angelika A   Leonard Thomas A TA  

Proceedings of the National Academy of Sciences of the United States of America 20230206 7

Phosphorylation is a ubiquitous mechanism by which signals are transduced in cells. Protein kinases, enzymes that catalyze the phosphotransfer reaction are, themselves, often regulated by phosphorylation. Paradoxically, however, a substantial fraction of more than 500 human protein kinases are capable of catalyzing their own activation loop phosphorylation. Commonly, these kinases perform this autophosphorylation reaction in <i>trans</i>, whereby transient dimerization leads to the mutual phosph  ...[more]

Similar Datasets

Proteomics ATP-competitive and allosteric inhibitors induce differential conformational changes at the autoinhibitory interface of Akt
2024-08-23 | PXD039028 | Pride
Proteomics Hydrogen Deuterium Exchange of PDK1
2022-05-20 | PXD027401 | Pride
Proteomics HDX-MS analysis of PI4Ka trimer and FAM126a (415-521) with calcineurin
2024-09-03 | PXD050633 | Pride
Proteomics Detailing the Structural and Dynamic Interactions Between WDR44 and Rab11
2023-03-11 | PXD035741 | Pride
Proteomics An HDX-MS optimised approach to characterise nanobodies as tools for biochemical and structural studies
2021-09-22 | PXD025207 | Pride
Proteomics Defining the molecular mechanism of PI4KA complex regulation by the phosphatase Calcineurin
2024-09-03 | PXD043409 | Pride
Proteomics Characterizing the Eaf complex using HDX-MS
2022-09-21 | PXD025715 | Pride
Proteomics Structure of the phosphoinositide 3-kinase p110-p101 complex reveals molecular mechanism of GPCR activation
2021-09-22 | PXD025209 | Pride
Proteomics HDX-MS analysis of PLIN3 membrane binding
2023-04-14 | PXD025717 | Pride
Proteomics Hydrogen Deuterium Exchange of PI4K(530-560) Peptide with Calcineurin
2024-09-03 | PXD044636 | Pride