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PXD065135-1

PXD065135 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe EGF receptor kinase domain is strongly activated by weak dimerization
DescriptionThe tyrosine kinase domain (TKD) of the epidermal growth factor receptor (EGFR) activates via a unique mechanism of asymmetric dimerization with a partner EGFR TKD rather than a more typical mechanism of activation loop phosphorylation. There is an EGFR oncogenic variant found in patients in which the TKD region of EGFR has been duplicated, resulting in a construct in which two EGFR kinase domain are linked via a natural peptide linker (KDD). KDD is the best approximation of the natural process of EGFR kinase dimerization and activation as well as an example of bona fide oncogenic activation. We studied the structure, enzyme properties, and structural dynamics of KDD to gather insights into the EGFR kinase activation process and its oncogenicity.
HostingRepositoryPRIDE
AnnounceDate2025-11-25
AnnouncementXMLSubmission_2025-11-25_06:15:39.115.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterZaritza Petrova
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationListNo PTMs are included in the dataset
InstrumentSynapt MS
Dataset History
RevisionDatetimeStatusChangeLog Entry
02025-06-17 19:40:15ID requested
12025-11-25 06:15:39announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: dynamics, KDD, dimerization, kinase, HDX-MS,EGFR
Contact List
Mark Lemmon
contact affiliationYale University, Yale Cancer Biology Institute
contact emailmark.lemmon@yale.edu
lab head
Zaritza Petrova
contact affiliationYale University
contact emailzaritza.petrova@yale.edu
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
Repository Record List
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