(Q27619043)

2

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J R Newcomb

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P E Rose

4

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D R Stover

5

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L M Toledo

6

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H Zhao

7

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K A Morgenstern

Differential signaling by lymphocyte antigen receptors.

8

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publication date

15 June 1999

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published in

Structure

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volume

7

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page(s)

651-61

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issue

6

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cites work

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Lymphocyte activation in health and disease

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T cell antigen receptor signal transduction

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The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase (p56lck) that phosphorylates the CD3 complex

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Genetic evidence of a role for Lck in T-cell receptor function independent or downstream of ZAP-70/Syk protein tyrosine kinases

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The p56lck SH2 domain mediates recruitment of CD8/p56lck to the activated T cell receptor/CD3/zeta complex.

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Association of CD8 with p56lck is required for early T cell signalling events.

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Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes

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Fidelity of T cell activation through multistep T cell receptor zeta phosphorylation

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Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists

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The CD3 chains of the T cell antigen receptor associate with the ZAP-70 tyrosine kinase and are tyrosine phosphorylated after receptor stimulation

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The zeta chain is associated with a tyrosine kinase and upon T-cell antigen receptor stimulation associates with ZAP-70, a 70-kDa tyrosine phosphoprotein

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ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity

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Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins

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Mechanism of activation for Zap-70 catalytic activity

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

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Adaptors and molecular scaffolds in immune cell signaling

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Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor

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p56lck signals for regulating thymocyte development can be distinguished by their dependency on Rho function

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The protein tyrosine kinase p56lck regulates thymocyte development independently of its interaction with CD4 and CD8 coreceptors [corrected]

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Profound block in thymocyte development in mice lacking p56lck

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Zinc is essential for binding of p56(lck) to CD4 and CD8alpha

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A Zn2+ ion links the cytoplasmic tail of CD4 and the N-terminal region of Lck

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The SH2 domain is required for stable phosphorylation of p56lck at tyrosine 505, the negative regulatory site

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Detection of a physical and functional interaction between Csk and Lck which involves the SH2 domain of Csk and is mediated by autophosphorylation of Lck on tyrosine 394

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Tyr394 and Tyr505 are autophosphorylated in recombinant Lck protein-tyrosine kinase expressed in Escherichia coli.

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The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions

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Crystal structure of the Src family tyrosine kinase Hck

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Three-dimensional structure of the tyrosine kinase c-Src

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Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement

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Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation

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Different susceptibility of protein kinases to staurosporine inhibition. Kinetic studies and molecular bases for the resistance of protein kinase CK2

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

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Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2

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Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine

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Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog

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A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket

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Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells

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