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High-Efficiency Expression and Solubilization of Functional T Cell Antigen Receptor Heterodimers
Isaac Engel, Tom H. M. Ottenhoff and Richard D. Klausner
New Series, Vol. 256, No. 5061 (May 29, 1992), pp. 1318-1321
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/2877309
Page Count: 4
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The T cell receptor (TCR) ζ chain was attached to the TCR α and β extracellular domains to induce efficient expression of αβ heterodimers that can recognize complexes of antigen with major histocompatibility complex (MHC) molecules. Chimeric constructs expressed in RBL-2H3 cells were efficiently transported to the cell surface uniquely as disulfide-linked heterodimers. Transfectants were activated by specific antigen-MHC complexes, which demonstrated that the expressed αβ was functional and that CD3 was not required for antigen-MHC binding. Constructs with thrombin cleavage sites were efficiently cleaved to soluble disulfide-linked heterodimers. Thus, attachment of TCR ζ domains and protease cleavage sites to TCR α and βinduces expression of demonstrably functional heterodimers that can be solubilized.
Science © 1992 American Association for the Advancement of Science