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PXD040765

PXD040765 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleAllosteric activation or inhibition of PI3Kγ mediated through conformational changes in the p110γ helical domain
DescriptionTo 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.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_05:52:23.261.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJohn Burke
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListphosphorylated residue
Instrumentimpact HD
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-03-10 04:41:46ID requested
12023-07-06 12:09:47announced
22024-10-22 05:52:23announced2024-10-22: Updated project metadata.
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: pi3k,hdx-ms, phosphorylation, hdx
Contact List
John Burke
contact affiliationUniversity of Victoria
contact emailjeburke@uvic.ca
lab head
John Burke
contact affiliationUniversity of Victoria
contact emailjeburke@uvic.ca
dataset submitter
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Dataset FTP location
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PRIDE project URI
Repository Record List
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