ArticleProtein science : a publication of the Protein Society2002
Competing modes of self-association in the regulatory domains of Bruton's tyrosine kinase: intramolecular contact versus asymmetric homodimerization.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 48 citations in OpenAlex.
- Membrane-dependent assembly of Bruton's tyrosine kinase mediated by the Proline-rich region and SH3 domain.Protein science : a publication of the Protein Society · 2025Article
- Article
- Conformational switches that control the TEC kinase - PLCγ signaling axis.Journal of structural biology: X · 2022Review
- Reining in BTK: Interdomain Interactions and Their Importance in the Regulatory Control of BTK.Frontiers in cell and developmental biology · 2021Review
- Dynamic regulatory features of the protein tyrosine kinases.Biochemical Society transactions · 2019Review
- Achieving a Graded Immune Response: BTK Adopts a Range of Active/Inactive Conformations Dictated by Multiple Interdomain Contacts.Structure (London, England : 1993) · 2017Article
- Dynamics of the Tec-family tyrosine kinase SH3 domains.Protein science : a publication of the Protein Society · 2016Article
- Autoinhibition of Bruton's tyrosine kinase (Btk) and activation by soluble inositol hexakisphosphate.eLife · 2015Article
- T-cell signaling regulated by the Tec family kinase, Itk.Cold Spring Harbor perspectives in biology · 2010Review
- Disrupting the intermolecular self-association of Itk enhances T cell signaling.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- SH2-dependent autophosphorylation within the Tec family kinase Itk.Journal of molecular biology · 2009Article
- Proline isomerization preorganizes the Itk SH2 domain for binding to the Itk SH3 domain.Journal of molecular biology · 2009Article
- Conformational snapshots of Tec kinases during signaling.Immunological reviews · 2009Article
- Backbone dynamics in an intramolecular prolylpeptide-SH3 complex from the diphtheria toxin repressor, DtxR.Journal of molecular biology · 2007Article
- Mechanism and functional significance of Itk autophosphorylation.Journal of molecular biology · 2007Article
- Quantitative relation between intermolecular and intramolecular binding of pro-rich peptides to SH3 domains.Biophysical journal · 2006Article
- Mimicry of a constitutively active pre-B cell receptor in acute lymphoblastic leukemia cells.The Journal of experimental medicine · 2005Article
- Btk is required for an efficient response to erythropoietin and for SCF-controlled protection against TRAIL in erythroid progenitors.The Journal of experimental medicine · 2004Article
- Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering.The EMBO journal · 2003Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
A nuclear magnetic resonance (NMR) investigation of a fragment of the nonreceptor Tec family tyrosine kinase Btk has revealed an intricate set of coupled monomer-dimer equilibria. The Btk fragment studied contains two consecutive proline-rich motifs followed by a single Src homology 3 (SH3) domain. We provide evidence for an asymmetric homodimer in which the amino-terminal proline sequence of one monomer contacts the opposite SH3 binding pocket, whereas the carboxy-terminal proline sequence of the other monomer is engaged by the second SH3 domain across the dimer interface. We show that the asymmetric homodimer structure is mimicked by a heterodimer formed in an equimolar mixture of complimentary mutants: one carrying mutations in the amino-terminal proline stretch; the other, in the carboxy-terminal proline motif. Moreover, a monomeric species characterized by an intramolecular complex between the amino-terminal proline motif and the SH3 domain predominates at low concentration. Association constants were determined for each of the competing equilibria by NMR titration. The similarity of the determined K(a) values reveals a delicate balance between the alternative conformational states available to Btk. Thus, changes in the local concentration of Btk itself, or co-localization with exogenous signaling molecules that have high affinity for either proline sequence or the SH3 domain, can significantly alter species composition and regulate Btk kinase 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.