Proteomics

Dataset Information

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Investigating the monomer-dimer transition of PKD1 kinase domain with EDC crosslinking

ABSTRACT: The project aim was to generate experimental constraints for the in silico modeling of the dimeric structure of the PKD kinase domain. And identify conformational changes upon dimerization. For this we used the heterobifunctional zero length crosslinker EDC to identify salt bridges within the protein and between the molecules in the dimeric arrangement. We could observe a stabilization of the protein in particularly in the activation loop upon dimerization and successfully identified one abundant dimer specific crosslink that helped us to identify contact surfaces in the dimer interface.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: WeiQiang Chen  

LAB HEAD: Thomas Leonard

PROVIDER: PXD031997 | Pride | 2023-03-11

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
20210415_QExHFX1_RSLC1_Reinhardt_Leonard_MPL_Dimer_band2_50p.raw Raw
20210415_QExHFX1_RSLC1_Reinhardt_Leonard_MPL_Monomer_band4_10p.raw Raw
20210419_Ronja_top8_proteins.fasta Fasta
Dimer_pLink_reports.zip Other
MQ_txt.zip Other
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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]

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