ArticleJournal of molecular biology2009
Proline isomerization preorganizes the Itk SH2 domain for binding to the Itk SH3 domain.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Purification and characterization of full-length monomeric TEC family kinase, ITK.Protein expression and purification · 2025Article
- Review
- The HIV-1 protein Nef activates the Tec family kinase Btk by stabilizing an intermolecular SH3-SH2 domain interaction.Science signaling · 2022Article
- Demonstration of Binding Induced Structural Plasticity in a SH2 Domain.Frontiers in molecular biosciences · 2020Article
- Regulation of Hematopoietic Cell Development and Function Through Phosphoinositides.Frontiers in immunology · 2018Review
- Dynamics of the Tec-family tyrosine kinase SH3 domains.Protein science : a publication of the Protein Society · 2016Article
- Calmodulin and PI(3,4,5)P₃ cooperatively bind to the Itk pleckstrin homology domain to promote efficient calcium signaling and IL-17A production.Science signaling · 2014Article
- Article
- Phosphotyrosine recognition domains: the typical, the atypical and the versatile.Cell communication and signaling : CCS · 2012Article
- Rescue of the aggregation prone Itk Pleckstrin Homology domain by two mutations derived from the related kinases, Btk and Tec.Protein science : a publication of the Protein Society · 2012Article
- Protein conformational switches: from nature to design.Chemistry (Weinheim an der Bergstrasse, Germany) · 2012Review
- Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII.Nature chemical biology · 2012Article
- Structure of the interleukin-2 tyrosine kinase Src homology 2 domain; comparison between X-ray and NMR-derived structures.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Two closely spaced tyrosines regulate NFAT signaling in B cells via Syk association with Vav.Molecular and cellular biology · 2011Article
- NMR reveals novel mechanisms of protein activity regulation.Protein science : a publication of the Protein Society · 2011Review
- Purification, crystallization and preliminary crystallographic analysis of the SH2 domain of IL-2-inducible T-cell kinase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Structural basis for regulation of the Crk signaling protein by a proline switch.Nature chemical biology · 2011Article
- T-cell signaling regulated by the Tec family kinase, Itk.Cold Spring Harbor perspectives in biology · 2010Review
- Loops govern SH2 domain specificity by controlling access to binding pockets.Science signaling · 2010Article
- Disrupting the intermolecular self-association of Itk enhances T cell signaling.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
We report here the NMR-derived structure of the binary complex formed by the interleukin-2 tyrosine kinase (Itk) Src homology 3 (SH3) and Src homology 2 (SH2) domains. The interaction is independent of both a phosphotyrosine motif and a proline-rich sequence, the classical targets of the SH2 and SH3 domains, respectively. The Itk SH3/SH2 structure reveals the molecular details of this nonclassical interaction and provides a clear picture for how the previously described prolyl cis/trans isomerization present in the Itk SH2 domain mediates SH3 binding. The higher-affinity cis SH2 conformer is preorganized to form a hydrophobic interface with the SH3 domain. The structure also provides insight into how autophosphorylation in the Itk SH3 domain might increase the affinity of the intermolecular SH3/SH2 interaction. Finally, we can compare this Itk complex with other examples of SH3 and SH2 domains engaging their ligands in a nonclassical manner. These small binding domains exhibit a surprising level of diversity in their binding repertoires.
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