PXD040765

PXD040765 is an original dataset announced via ProteomeXchange.

Title	Allosteric activation or inhibition of PI3Kγ mediated through conformational changes in the p110γ helical domain
Description	To provide additional insight into the molecular mechanisms underlying p110 phosphorylation we carried out hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments on p110 and phosphorylated p110 (90.8% phosphorylated S594/595, 92% phosphorylated S582. When we compared phosphorylated p110 (>90.8% as measured by mass spectrometry at both sites) to unphosphorylated p110 we observed extensive increases in dynamics in the C2, helical domain and kinase domain (Fig. 4A-D). The largest increases in exchange upon phosphorylation were located in the N-terminal region of the helical domain, with the peptides directly adjacent to the phosphorylation site showing almost complete deuterium incorporation at the earliest time points of exchange. This is indicative of significant disruption of the alpha helical secondary structure in this region.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:52:23.261.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	John Burke
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue
Instrument	impact HD

Revision	Datetime	Status	ChangeLog Entry
0	2023-03-10 04:41:46	ID requested
1	2023-07-06 12:09:47	announced
⏵ 2	2024-10-22 05:52:23	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: pi3k,hdx-ms, phosphorylation, hdx

John Burke
contact affiliation	University of Victoria
contact email	jeburke@uvic.ca
lab head
John Burke
contact affiliation	University of Victoria
contact email	jeburke@uvic.ca
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD040765
     1. Label: PRIDE project
     2. Name: Allosteric activation or inhibition of PI3Kγ mediated through conformational changes in the p110γ helical domain