Phosphorylated T Cell Receptor ζ-Chain and ZAP70 Tandem SH2 Domains Form a 1:3 Complex In Vitro

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Phosphorylated T Cell Receptor ζ-Chain and ZAP70 Tandem SH2 Domains Form a 1:3 Complex In Vitro

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Title: Phosphorylated T Cell Receptor ζ-Chain and ZAP70 Tandem SH2 Domains Form a 1:3 Complex In Vitro
Author: Eck, Michael; Weissenhorn, Winfried; Wiley, Don C.; Harrison, Stephen C.

Note: Order does not necessarily reflect citation order of authors.

Citation: Weissenhorn, Winfried, Michael J. Eck, Stephen C. Harrison, and Don C. Wiley. 1996. Phosphorylated T cell receptor ζ-chain and ZAP70 tandem SH2 domains form a 1:3 complex in vitro. European Journal of Biochemistry 238: 440-445.
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Abstract: The ζ polypeptide is part of the T cell antigen receptor (TCR). The ζ-chain contributes to efficient cell-surface expression of the TCR and accounts for part of its signal transduction capability. TCR recognition triggers a complex set of events that result in cellular activation. The protein tyrosine kinase (PTK) Lck phosphorylates the ζ-chain, which in turn associates with another PTK, ZAP70, and stimulates its phosphorylation activity. Here we report the expression of the intracellular part of the ζ-chain and its biochemical characterization. The recombinant protein does not dimerize by itself in solution. Circular-dichroic analysis reveals a random coil conformation. ζ, phosphorylated using recombinant Lck, associates with recombinant ZAP70 tandem-SH2 domains. All three T cell activation motifs in ζ bind ZAP70 tandem-SH2 domains in vitro, forming a 1:3 complex. This result extends the picture, derived from earlier studies, of a mechanism for signal amplification.
Published Version: http://www3.interscience.wiley.com/cgi-bin/fulltext/119201049/PDFSTART
Other Sources: http://crystal.harvard.edu/lib-sch/Weissen-1996-EJBioc-238-440.pdf
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:3322468

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  • FAS Scholarly Articles [6463]
    Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University
 
 

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