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
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.
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“Binding of ZAP-70 to ITAM motifs of CD3ζ has been suggested to induce a conformational change of ZAP-70 to facilitate the phosphorylation of Tyr315 and Tyr319 in interdomain B of ZAP-70, which establishes and stabilizes the active conformation of ZAP-70[17], [34].”
From RhoH Regulates Subcellular Localization of ZAP-70 and Lck in T Cell Receptor Signaling (2010) · cites this paper as [34]
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RhoH Regulates Subcellular Localization of ZAP-70 and Lck in T Cell Receptor Signaling
Chae, H.-D., Siefring, J. E., Hildeman, D. A., Gu, Y., & Williams, D. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013970 · Cited by 35
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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
- Cited by
- 234
- References
- 47
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2305 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
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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.
