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PMID: 2974063 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The lysine residue in the membrane-spanning domain of the beta chain is necessary for cell surface expression of the T cell antigen receptor.

The Journal of experimental medicine ·Vol. 168 ·No. 6 ·1988-12-01 ·Pages 1971-8

Morley BJ, Chin KN, Newton ME, Weiss A

Abstract

The TCR is a complex receptor composed of seven polypeptide chains consisting of a ligand-binding subunit, Ti, and a putative signal-transducing subunit, CD3. Phylogenetically conserved charged amino acid residues within the membrane-spanning domains present in all seven chains of the TCR have been proposed to be important in the association between Ti and CD3. Using a Ti beta chain-deficient mutant of the cell line Jurkat, site-directed mutagenesis and transfection of Ti beta chain cDNA was performed to assess the importance of the lysine residue at position 290 within the membrane-spanning domain of the Ti beta chain to expression of the TCR complex. These studies demonstrated that the lysine residue, and not simply conservation of either basic charge or secondary structure, is important at this position.

MeSH Terms
Blotting, Northern Cell Line Cell Membrane/metabolism Flow Cytometry Humans Lysine Mutation Receptors, Antigen, T-Cell/metabolism Receptors, Antigen, T-Cell, alpha-beta Transfection
Chemicals
Receptors, Antigen, T-Cell Receptors, Antigen, T-Cell, alpha-beta Lysine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Morley B J
Howard Hughes Medical Institute, Department of Medicine, University of California, San Francisco 94143.
Chin K N
Newton M E
Weiss A
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Article Info
Journal
The Journal of experimental medicine
Abbr.
J Exp Med
ISSN
0022-1007
Published
1988-12-01
Pages
1971-8
Language
English
Region
United States
NLM ID
2985109R
PMCID
PMC2189156
Subset
IM
Grants
NIGMS NIH HHS · GM-39553-01 · United States
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