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

FEBS Letters

Vihinen, Mauno²  Smith, C.I.Edvard⁴  Okoh, Michael P¹  Hansson, Henrik³  Härd, Torleif³ 

[1] Institute of Medical Technology, University of Tampere, P.O. Box 607, FIN-33101 Tampere, Finland;Department of Biosciences, Division of Biochemistry, University of Helsinki, P.O. Box 56, FIN-00014 Helsinki, Finland;Department of Biotechnology, Royal Institute of Technology(KTH), Center for Structural Biochemistry, Novum, S-141 57 Huddinge, Sweden;Department of Biosciences at Novum, Karolinska Institute, S-141 57 Huddinge, Sweden

关键词: Bruton's tyrosine kinase;    Src homology 3;    Dimerization;    Nuclear magnetic resonance;    Gel permeation chromatography;    Signal transduction;    Btk;    Bruton's tyrosine kinase;    SH3 domain;    Src homology 3 domain;    TH region;    Tec homology region;    PRR-SH3;    N-terminally extended Btk SH3 domain containing the proline-rich sequences of the TH region;    NMR;    nuclear magnetic resonance;    GPC;    gel permeation chromatography;   

DOI  :  10.1016/S0014-5793(00)02438-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 ¹⁵N NMR relaxation measurements are all consistent with a monomer–dimer equilibrium with a dissociation constant on the order of 60 μM. 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.

【 授权许可】

Unknown