Authors: | Call, M. E.; Pyrdol, J.; Wiedmann, M.; Wucherpfennig, K. W. |
Article Title: | The organizing principle in the formation of the T cell receptor-CD3 complex |
Abstract: | The T cell receptor (TCR) serves a critical function in the immune system and represents one of the most complex receptor structures. A striking feature is the presence of nine highly conserved, potentially charged residues in the transmembrane helices. Previous models have attempted to explain assembly based on pairwise interactions of these residues. Using a novel method for the isolation of intact radiolabeled protein complexes, we demonstrate that one basic and two acidic transmembrane residues are required for the assembly of each of the three signaling dimers with the TCR. This remarkable three-helix arrangement applies to all three assembly steps and represents the organizing principle for the formation of this intricate receptor structure. |
Keywords: | signal transduction; controlled study; human cell; protein domain; protein motif; cd3 antigen; t-lymphocytes; complex formation; protein protein interaction; t lymphocyte receptor; cell membrane; immunoprecipitation; dimerization; protein structure, tertiary; amino acids; protein structure; protein structure, secondary; macromolecular substances; protein isolation; humans; human; priority journal; article; receptor-cd3 complex, antigen, t-cell |
Journal Title: | Cell |
Volume: | 111 |
Issue: | 7 |
ISSN: | 0092-8674 |
Publisher: | Cell Press |
Date Published: | 2002-12-27 |
Start Page: | 967 |
End Page: | 979 |
Language: | English |
DOI: | 10.1016/s0092-8674(02)01194-7 |
PUBMED: | 12507424 |
PROVIDER: | scopus |
PMCID: | PMC3420808 |
DOI/URL: | |
Notes: | Export Date: 14 November 2014 -- Source: Scopus |