biostudies-literatureSun ZYNIAID NIH HHSNIGMS NIH HHS16867-72https://www.ebi.ac.uk/biostudies/studies/S-EPMC534738biostudies-literatureUnknown101(48)Invariant CD3 subunit dimers (CD3epsilongamma, CD3epsilondelta, and CD3zetazeta) are the signaling components of the alphabeta T cell receptor (TCR). The recently solved structure of murine CD3epsilongamma revealed a unique side-to-side interface and central beta-sheets conjoined between the two C2-set Ig-like ectodomains, with the pairing of the parallel G strands implying a potential concerted piston-type movement for signal transduction. Although CD3gamma and CD3delta each dimerize with CD3epsilon, there are differential CD3 subunit requirements for receptor assembly and signaling among T lineage subpopulations, presumably mandated by structural differences. Here we present the solution structure of the heterodimeric CD3epsilondelta complex. Whereas the CD3epsilon subunit conformation iProceedings of the National Academy of Sciences of the United States of AmericaSolution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.PMC534738R01 AI019807P01 GM047467R01 AI037581R56 AI019807GM47467AI19807R37 AI019807AI37581Sun ZYWagner GKim STReinherz ELFahmy AKim ICfalseSolution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.Invariant CD3 subunit dimers (CD3epsilongamma, CD3epsilondelta, and CD3zetazeta) are the signaling components of the alphabeta T cell receptor (TCR). The recently solved structure of murine CD3epsilongamma revealed a unique side-to-side interface and central beta-sheets conjoined between the two C2-set Ig-like ectodomains, with the pairing of the parallel G strands implying a potential concerted piston-type movement for signal transduction. Although CD3gamma and CD3delta each dimerize with CD3epsilon, there are differential CD3 subunit requirements for receptor assembly and signaling among T lineage subpopulations, presumably mandated by structural differences. Here we present the solution structure of the heterodimeric CD3epsilondelta complex. Whereas the CD3epsilon subunit conformation i2004-01-01T00:00:00Z2004 Nov2026-05-01T21:44:51.721Z2019-03-27T01:08:24ZS-EPMC5347381555700110.1073/pnas.0407576101