Show simple item record

dc.contributor.authorMarasco, Michelangelo
dc.contributor.authorKirkpatrick, John P
dc.contributor.authorCarlomagno, Teresa
dc.date.accessioned2020-05-25T11:26:19Z
dc.date.available2020-05-25T11:26:19Z
dc.date.issued2020-04-01
dc.identifier.citationBiomol NMR Assign. 2020;10.1007/s12104-020-09941-y. doi:10.1007/s12104-020-09941-yen_US
dc.identifier.pmid32236803
dc.identifier.doi10.1007/s12104-020-09941-y
dc.identifier.urihttp://hdl.handle.net/10033/622269
dc.description.abstractInhibition of immune checkpoint receptor Programmed Death-1 (PD-1) via monoclonal antibodies is an established anticancer immunotherapeutic approach. This treatment has been largely successful; however, its high cost demands equally effective, more affordable alternatives. To date, the development of drugs targeting downstream players in the PD-1-dependent signaling pathway has been hampered by our poor understanding of the molecular details of the intermolecular interactions involved in the pathway. Activation of PD-1 leads to phosphorylation of two signaling motifs located in its cytoplasmic domain, the immune tyrosine inhibitory motif (ITIM) and immune tyrosine switch motif (ITSM), which recruit and activate protein tyrosine phosphatase SHP2. This interaction is mediated by the two Src homology 2 (SH2) domains of SHP2, termed N-SH2 and C-SH2, which recognize phosphotyrosines pY223 and pY248 of ITIM and ITSM, respectively. SHP2 then propagates the inhibitory signal, ultimately leading to suppression of T cell functionality. In order to facilitate mechanistic structural studies of this signaling pathway, we report the resonance assignments of the complexes formed by the signaling motifs of PD-1 and the SH2 domains of SHP2.en_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectImmunotherapyen_US
dc.subjectPD-1en_US
dc.subjectSH2 domainsen_US
dc.subjectSHP2en_US
dc.title1H, 13C, 15N chemical shift assignments of SHP2 SH2 domains in complex with PD-1 immune-tyrosine motifs.en_US
dc.typeArticleen_US
dc.identifier.eissn1874-270X
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalBiomolecular NMR assignmentsen_US
refterms.dateFOA2020-05-25T11:26:21Z
dc.source.journaltitleBiomolecular NMR assignments
dc.source.countryNetherlands


Files in this item

Thumbnail
Name:
Marasco, Kirkpatrick and Carlo ...
Size:
3.185Mb
Format:
PDF
Description:
Open Access publication

This item appears in the following Collection(s)

Show simple item record

Attribution-NonCommercial-ShareAlike 4.0 International
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 4.0 International