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

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Author

Summary, in English

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.

Publishing year

2001

Language

English

Pages

67-70

Publication/Series

FEBS Letters

Volume

489

Issue

1

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Biological Sciences

Keywords

  • Bruton's tyrosine kinase
  • Src homology 3
  • dimerization
  • nuclear magnetic
  • resonance
  • gel permeation chromatography
  • signal transduction

Status

Published

ISBN/ISSN/Other

  • ISSN: 1873-3468