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Updated: Jan 29, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
Published on: June 19, 2010
A structural model of the immune checkpoint CD160-HVEM complex derived from HDX-mass spectrometry and molecular
Katarzyna Kuncewicz1, Marta Spodzieja1, Adam Sieradzan2
1University of Gdansk, Faculty of Chemistry, Department of Biomedical Chemistry, Gdansk, Poland.
Abstract:
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.
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