<<< Full experiment listing


PXD014348 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleGeneral structural features that regulate integrin affinity revealed by atypical αVβ8
DescriptionIntegrins αVβ8 and αVβ6 are master activators of proTGF-βs. Whereas most integrins including αVβ6 are activated by tensile force applied by the cytoskeleton, αVβ8 links differently to the cytoskeleton and lacks the open headpiece conformation that represents the high affinity state of other integrins. Here, we shed light on the atypical activation mechanism of integrin αVβ8 using crystal structures in the absence and presence of proTGF-β1 peptide, comparisons of the hydrogen deuterium exchange dynamics of αVβ8 and αVβ6, and affinity measurements on mutants in which structurally atypical residues of αVβ8 and typical residues of αVβ6 were reciprocally exchanged.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJohn R. Engen
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListNo PTMs are included in the dataset
InstrumentSynapt MS
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-06-24 02:35:02ID requested
12019-12-03 12:13:40announced
22020-01-13 05:23:20announced2020-01-13: Updated publication reference for PubMed record(s): 31792290.
Publication List
Wang J, Su Y, Iacob RE, Engen JR, Springer TA, 8. Nat Commun, 10(1):5481(2019) [pubmed]
Keyword List
submitter keyword: Integrin, proTGF-β, Crystal structure, Affinity, Conformational change, hydrogen deuterium exchange
Contact List
John R. Engen
contact affiliationChemistry & Chemical Biology, Northeastern University
contact emailj.engen@northeastern.edu
lab head
John R. Engen
contact affiliationNortheastern University
contact emailj.engen@northeastern.edu
dataset submitter
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/12/PXD014348
PRIDE project URI
Repository Record List
[ + ]