{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sun ZY"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["16867-72"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC534738"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["101(48)"],"pubmed_abstract":["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 i"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Solution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling."],"pmcid":["PMC534738"],"funding_grant_id":["R01 AI019807","P01 GM047467","R01 AI037581","R56 AI019807","GM47467","AI19807","R37 AI019807","AI37581"],"pubmed_authors":["Sun ZY","Wagner G","Kim ST","Reinherz EL","Fahmy A","Kim IC"],"additional_accession":[]},"is_claimable":false,"name":"Solution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.","description":"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 i","dates":{"release":"2004-01-01T00:00:00Z","publication":"2004 Nov","modification":"2026-05-01T21:44:51.721Z","creation":"2019-03-27T01:08:24Z"},"accession":"S-EPMC534738","cross_references":{"pubmed":["15557001"],"doi":["10.1073/pnas.0407576101"]}}