A structural model of the immune checkpoint CD160-HVEM complex derived from HDX-mass spectrometry and molecular modeling.
Fiche du document
11 janvier 2019
- doi: 10.18632/oncotarget.26570
- issn: 1949-2553
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.18632/oncotarget.26570
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/30728903
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/eissn/1949-2553
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_F79CFFA532C99
info:eu-repo/semantics/openAccess , CC BY 4.0 , https://creativecommons.org/licenses/by/4.0/
Sujets proches
Mass spectroscopy Mass spectra Mass spectrograph Mass spectrum analysisCiter ce document
K. Kuncewicz et al., « A structural model of the immune checkpoint CD160-HVEM complex derived from HDX-mass spectrometry and molecular modeling. », Serveur académique Lausannois, ID : 10.18632/oncotarget.26570
Métriques
Partage / Export
Résumé
CD160 is a T cell coinhibitory molecule that interacts with the herpes virus entry mediator (HVEM) on antigen-presenting cells to provide an inhibitory signal to T cells. To date, the structure of CD160 and its complex with HVEM are unknown. Here, we have identified the fragments of CD160 interacting with HVEM using ELISA tests, hydrogen/deuterium studies, affinity chromatography and mass spectrometry (MS). By combining hydrogen/deuterium exchange and mass spectrometry (HDX-MS) we obtained key information about the tertiary structure of CD160, predicting the 3D structure of the CD160-HVEM complex. Our results provide insights into the molecular architecture of this complex, serving as a useful basis for designing inhibitors for future immunotherapies.