{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Call ME"],"funding":["NIBIB NIH HHS","NIAID NIH HHS","PHS HHS"],"pagination":["355-68"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3466601"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["127(2)"],"pubmed_abstract":["The T cell receptor (TCR) alphabeta heterodimer communicates ligand binding to the cell interior via noncovalently associated CD3gammaepsilon, CD3deltaepsilon, and zetazeta dimers. While structures of extracellular components of the TCR-CD3 complex are known, the transmembrane (TM) domains that mediate assembly have eluded structural characterization. Incorporation of the zetazeta signaling module is known to require one basic TCRalpha and two zetazeta aspartic acid TM residues. We report the NMR structure of the zetazeta(TM) dimer, a left-handed coiled coil with substantial polar contacts. Mutagenesis experiments demonstrate that three polar positions are critical for zetazeta dimerization and assembly with TCR. The two aspartic acids create a single structural unit at the zetazeta interf"],"journal":["Cell"],"pubmed_title":["The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor."],"pmcid":["PMC3466601"],"funding_grant_id":["F32","P41 EB002026","R01 AI054520","EB002026"],"pubmed_authors":["Call ME","Schnell JR","Wucherpfennig KW","Xu C","Lutz RA","Chou JJ"],"additional_accession":[]},"is_claimable":false,"name":"The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor.","description":"The T cell receptor (TCR) alphabeta heterodimer communicates ligand binding to the cell interior via noncovalently associated CD3gammaepsilon, CD3deltaepsilon, and zetazeta dimers. While structures of extracellular components of the TCR-CD3 complex are known, the transmembrane (TM) domains that mediate assembly have eluded structural characterization. Incorporation of the zetazeta signaling module is known to require one basic TCRalpha and two zetazeta aspartic acid TM residues. We report the NMR structure of the zetazeta(TM) dimer, a left-handed coiled coil with substantial polar contacts. Mutagenesis experiments demonstrate that three polar positions are critical for zetazeta dimerization and assembly with TCR. The two aspartic acids create a single structural unit at the zetazeta interf","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Oct","modification":"2026-05-05T01:40:12.688Z","creation":"2026-04-07T21:14:42.597Z"},"accession":"S-EPMC3466601","cross_references":{"pubmed":["17055436"],"doi":["10.1016/j.cell.2006.08.044"]}}