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PMID: 12507424 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The organizing principle in the formation of the T cell receptor-CD3 complex.

Cell ·Vol. 111 ·No. 7 ·2002-12-27 ·Pages 967-79

Call ME, Pyrdol J, Wiedmann M, Wucherpfennig KW

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.

MeSH Terms
Amino Acids/chemistry Cell Membrane/chemistry,immunology Dimerization Humans Macromolecular Substances Protein Structure, Secondary/physiology Protein Structure, Tertiary/physiology Receptor-CD3 Complex, Antigen, T-Cell/immunology,isolation & purification T-Lymphocytes/chemistry,immunology
Chemicals
Amino Acids Macromolecular Substances Receptor-CD3 Complex, Antigen, T-Cell
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Call Matthew E
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, MA 02115, USA.
Pyrdol Jason
Wiedmann Martin
Wucherpfennig Kai W
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Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
2002-12-27
Pages
967-79
Language
English
Region
United States
NLM ID
0413066
PMCID
PMC3420808
Subset
IM
Grants
NIAID NIH HHS · P01 AI045757 · United States
NINDS NIH HHS · R01 NS039096 · United States
NIAID NIH HHS · AI45757 · United States
NINDS NIH HHS · NS39096 · United States
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