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
| 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. |
| Full Text & Related Files: |
Harrison_PhosphorylatedTCell.pdf (521.4Kb; PDF) 
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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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Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University
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