Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase

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Abstract

The SH3 domain of Bruton's tyrosine kinase (Btk) is preceded by the Tec homology (TH) region containing proline-rich sequences. We have studied a protein fragment containing both the Btk SH3 domain and the proline-rich sequences of the TH region (PRR-SH3). Intermolecular NMR cross-relaxation measurements, gel permeation chromatography profiles, titrations with proline-rich peptides, and N-15 NMR relaxation measurements are all consistent with a monomer-dimer equilibrium with a dissociation constant on the order of 60 muM. The intermolecular interactions do, at least in part, involve proline-rich sequences in the TH region. This behavior of Btk PRR-SH3 may have implications for the functional action of Btk. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

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Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences

Keywords

  • Bruton's tyrosine kinase, Src homology 3, dimerization, nuclear magnetic, resonance, gel permeation chromatography, signal transduction
Original languageEnglish
Pages (from-to)67-70
JournalFEBS Letters
Volume489
Issue number1
Publication statusPublished - 2001
Publication categoryResearch
Peer-reviewedYes
Externally publishedYes