Proteomics

Dataset Information

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Analyzing Intrinsically Ordered and Disordered Regions of the DDD Complex

ABSTRACT: We used HDX-MS to analyze which regions of the DDD complex are intrinsically ordered and disordered. Deuterium incorporation after 3 seconds at zero degrees celsius was compared to deuterium incoporation in a fully deuterated sample. We were able to determine which componants of the DDD complex have the most stable and unstable secondary structure.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD057548 | Pride | 2025-03-10

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
07_15_24_TL_Ord-v-Disord_DD-MSMS.d.rar Other
07_16_24_TL_DD-FD.d.rar Other
07_16_24_TL_DD_3s-1.d.rar Other
07_16_24_TL_DD_3s-2.d.rar Other
07_16_24_TL_DD_3s-3.d.rar Other
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Publications

DET1 dynamics underlie cooperative ubiquitination by CRL4<sup>DET1-COP1</sup> complexes.

Burgess Abigail E AE   Loughran Tarren A TA   Turk Liam S LS   Nyvall Hunter G HG   Dunlop Jessica L JL   Jamieson Sam A SA   Curry Jack R JR   Burke John E JE   Filipcik Pavel P   Brown Simon H J SHJ   Mace Peter D PD  

Science advances 20250226 9

Transcription factor ubiquitination is a decisive regulator of growth and development. The DET1-DDB1-DDA1 (DDD) complex associates with the Cullin-4 ubiquitin ligase (CRL4) and a second ubiquitin ligase, COP1, to control ubiquitination of transcription factors involved in neurological, metabolic, and immune cell development. Here, we report the structure of the human DDD complex, revealing a specific segment of DET1 that can recruit ubiquitin-conjugating (E2) enzymes. Structural variability anal  ...[more]

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