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Cited by 234

The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.

Structural Basis for the Inhibition of Tyrosine Kinase Activity of ZAP-70

Deindl, Sebastian, Kadlecek, Theresa A., Brdicka, Tomas, Cao, Xiaoxian, Weiss, Arthur, Kuriyan, John·2007·Cell
DOI 10.1016/j.cell.2007.03.039
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Abstract

ZAP-70, a cytoplasmic tyrosine kinase required for T cell antigen receptor signaling, is controlled by a regulatory segment that includes a tandem SH2 unit responsible for binding to immunoreceptor tyrosine-based activation motifs (ITAMs). The crystal structure of autoinhibited ZAP-70 reveals that the inactive kinase domain adopts a conformation similar to that of cyclin-dependent kinases and Src kinases. The autoinhibitory mechanism of ZAP-70 is, however, distinct and involves interactions between the regulatory segment and the hinge region of the kinase domain that reduce its flexibility. Two tyrosine residues in the SH2-kinase linker that activate ZAP-70 when phosphorylated are involved in aromatic-aromatic interactions that connect the linker to the kinase domain. These interactions are inconsistent with ITAM binding, suggesting that destabilization of this autoinhibited ZAP-70 conformation is the first step in kinase activation.

Overview

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Crossref · 10.1016/j.cell.2007.03.039

Cites

47 of 47 references verified0 citation errors · 0 not checkable

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Citations

Cites

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Metadata

Authors
Deindl, S., Kadlecek, T. A., Brdicka, T., Cao, X., Weiss, A., & Kuriyan, J.
Venue
Cell
Publisher
Elsevier BV
Published
2007-05
Volume
129
Issue
4
Pages
735-746
ISSN
0092-8674
DOI
10.1016/j.cell.2007.03.039
Cited by
234
References
47
Language
en
Licence

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Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.