Interaction between the SH2 domains of ZAP-70 and the tyrosine-based activation motif 1 sequence of the zeta subunit of the T-cell receptor

Archives of Biochemistry and Biophysics
M E LabadiaR H Ingraham

Abstract

One of the key steps involved in T-cell activation is binding of the tyrosine kinase ZAP-70 via its two SH2 domains to peptide segments termed tyrosine-based activation motifs (ITAM) which are present in three of the T-cell receptor (TCR) subunits. The crystal structure of the ZAP-70 SH2 domains complexed to phosphopeptide revealed that the amino-terminal phosphotyrosine-binding pocket is formed at the interface between the two SH2 domains. This study was designed to further characterize the binding between TCR zeta ITAM1 and the ZAP-70 SH2 domains as well as to assess the change in conformation of SH2 domain structure upon zeta ITAM1 binding. BIAcore analysis of wild type and nonfunctional single-point mutants of ZAP-70 SH2 domains demonstrated that the amino-terminal SH2 domain can bind phosphopeptide in the absence of a functional carboxyl-terminal SH2 domain. In addition, the amino-terminal SH2 domain prefers the RREEpYDVLDK sequence of zeta chain ITAM1 over the GQNQLpYNELNL sequence. To assess changes in protein conformation upon ITAM binding to ZAP-70 SH2 domains, fluorescence spectroscopy and analytical ultracentrifugation experiments were performed. A significant blue shift in the tryptophan emission spectrum of the SH2...Continue Reading

References

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Citations

Dec 8, 2010·Proceedings of the National Academy of Sciences of the United States of America·Ivan A Yudushkin, Ronald D Vale
May 24, 2011·The Journal of Biological Chemistry·Peter J Bond, José D Faraldo-Gómez
Apr 7, 2000·Protein Science : a Publication of the Protein Society·R O'BrienJ E Ladbury
Jan 20, 2016·The Journal of Experimental Medicine·Alice Y ChanJennifer M Puck
Mar 24, 2020·The Biochemical Journal·Kaustav GangopadhyayRahul Das
Jul 5, 2002·The Journal of Immunology : Official Journal of the American Association of Immunologists·Einar Martin AandahlDouglas F Nixon

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