The three-dimensional structure of the ZAP-70 kinase domain in complex with staurosporine: implications for the design of selective inhibitors. (Q45005856)

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

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31 December 2019

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

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31 December 2019

Michael J. Rynkiewicz

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31 December 2019

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Lei Jin

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31 December 2019

Scott Pluskey

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31 December 2019

Eugene C Petrella

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31 December 2019

Susan M Cantin

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31 December 2019

Joan C Gorga

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Pramod Pandey

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31 December 2019

James E Strickler

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31 December 2019

Robert E Babine

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31 December 2019

David T Weaver

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31 December 2019

Katherine J Seidl

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29 July 2004

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31 December 2019

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Journal of Biological Chemistry

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31 December 2019

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42818-42825

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31 December 2019

Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor

1 reference

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21 January 2018

Activation of T cells by a tyrosine kinase activation domain in the cytoplasmic tail of CD3 epsilon.

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ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain

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Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase

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ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency

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F2(Pmp)2-TAM zeta 3, a novel competitive inhibitor of the binding of ZAP-70 to the T cell antigen receptor, blocks early T cell signaling

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Signal transduction mediated by the T-cell antigen receptor

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A peptide library approach identifies a specific inhibitor for the ZAP-70 protein tyrosine kinase

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Activating and inhibitory mutations in adjacent tyrosines in the kinase domain of ZAP-70.

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Homogeneous proximity tyrosine kinase assays: scintillation proximity assay versus homogeneous time-resolved fluorescence.

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Processing of X-ray diffraction data collected in oscillation mode

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Activation of Zap-70 tyrosine kinase due to a structural rearrangement induced by tyrosine phosphorylation and/or ITAM binding

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28 Use and specificity of staurosporine, UCN-O1, and calphostin C as protein kinase inhibitors

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Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential

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Structures of staurosporine bound to CDK2 and cAPK--new tools for structure-based design of protein kinase inhibitors

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Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors

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