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

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.

• Författare: H Hansson; MP Okoh; CIE Smith; Mauno Vihinen; T Hard
• Publiceringsår: 2001
• Språk: Engelska
• Sidor: 67-70
• Publikation/Tidskrift/Serie: FEBS Letters
• Volym: 489
• Issue: 1
• Länkar: http://dx.doi.org/10.1016/S0014-5793(00)02438-8
• Dokumenttyp: Artikel i tidskrift
• Förlag: Wiley-Blackwell
• Ämne: Biological Sciences
• Nyckelord: Bruton's tyrosine kinase; Src homology 3; dimerization; nuclear magnetic; resonance; gel permeation chromatography; signal transduction
• Status: Published
• ISBN/ISSN/Övrigt: ISSN: 1873-3468