The three-dimensional structure of the ZAP-70 kinase domain in complex with staurosporine: implications for the design of selective inhibitors.

@article{Jin2004TheTS,
  title={The three-dimensional structure of the ZAP-70 kinase domain in complex with staurosporine: implications for the design of selective inhibitors.},
  author={Lei Jin and Scott Pluskey and Eugene C Petrella and Susan M Cantin and Joan C. Gorga and Michael J. Rynkiewicz and Pramod Pandey and James E. Strickler and Robert E. Babine and David T. Weaver and Katherine J. Seidl},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 41},
  pages={42818-25}
}
The ZAP-70 tyrosine kinase plays a critical role in T cell activation and the immune response and therefore is a logical target for immunomodulatory therapies. Although the crystal structure of the tandem Src homology-2 domains of human ZAP-70 in complex with a peptide derived from the zeta subunit of the T cell receptor has been reported (Hatada, M. H., Lu, X., Laird, E. R., Green, J., Morgenstern, J. P., Lou, M., Marr, C. S., Phillips, T. B., Ram, M. K., Theriault, K., Zoller, M. J., and… CONTINUE READING

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