ArticleThe EMBO journal2003
Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 78 citations in OpenAlex.
- Mechanism of activation of an ancestral TEC kinase by PIPNpj structural biology · 2026Article
- Article
- Acquired BTK mutations associated with resistance to noncovalent BTK inhibitors.Blood advances · 2023Article
- Conformational switches that control the TEC kinase - PLCγ signaling axis.Journal of structural biology: X · 2022Review
- Diffusion-based determination of protein homodimerization on reconstituted membrane surfaces.BMB reports · 2021Review
- Structure-Function Relationships of Covalent and Non-Covalent BTK Inhibitors.Frontiers in immunology · 2021Review
- Reining in BTK: Interdomain Interactions and Their Importance in the Regulatory Control of BTK.Frontiers in cell and developmental biology · 2021Review
- Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms.Nature communications · 2020Article
- Noncatalytic Bruton's tyrosine kinase activates PLCγThe Journal of biological chemistry · 2020Article
- Dynamic regulatory features of the protein tyrosine kinases.Biochemical Society transactions · 2019Review
- Differential Conformational Dynamics Encoded by the Linker between Quasi RNA Recognition Motifs of Heterogeneous Nuclear Ribonucleoprotein H.Journal of the American Chemical Society · 2018Article
- Achieving a Graded Immune Response: BTK Adopts a Range of Active/Inactive Conformations Dictated by Multiple Interdomain Contacts.Structure (London, England : 1993) · 2017Article
- An Autoinhibitory Role for the Pleckstrin Homology Domain of Interleukin-2-Inducible Tyrosine Kinase and Its Interplay with Canonical Phospholipid Recognition.Biochemistry · 2017Article
- Crystal structure of an SH2-kinase construct of c-Abl and effect of the SH2 domain on kinase activity.The Biochemical journal · 2015Article
- Autoinhibition of Bruton's tyrosine kinase (Btk) and activation by soluble inositol hexakisphosphate.eLife · 2015Article
- The SH2 domain regulates c-Abl kinase activation by a cyclin-like mechanism and remodulation of the hinge motion.PLoS computational biology · 2014Article
- Substrate-specific reorganization of the conformational ensemble of CSK implicates novel modes of kinase function.PLoS computational biology · 2012Article
- Proteins at work: a combined small angle X-RAY scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscape.The Journal of biological chemistry · 2010Article
- T-cell signaling regulated by the Tec family kinase, Itk.Cold Spring Harbor perspectives in biology · 2010Review
- Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering.European biophysics journal : EBJ · 2010Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brutons's tyrosine kinase (Btk) is a non-receptor protein tyrosine kinase (nrPTK) essential for the development of B lymphocytes in humans and mice. Like Src and Abl PTKs, Btk contains a conserved cassette formed by SH3, SH2 and protein kinase domains, but differs from them by the presence of an N-terminal PH domain and the Tec homology region. The domain structure of Btk was analysed using X-ray synchrotron radiation scattering in solution. Low resolution shapes of the full-length protein and several deletion mutants determined ab initio from the scattering data indicated a linear arrangement of domains. This arrangement was further confirmed by rigid body modelling using known high resolution structures of individual domains. The final model of Btk displays an extended conformation with no, or little, inter-domain interactions. In agreement with these results, deletion of non-catalytic domains failed to enhance the activity of Btk. Taken together, our results indicate that, contrary to Src and Abl, Btk might not require an assembled conformation for the regulation of its activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.