Hansson H, Okoh M P, Smith C I, Vihinen M, Härd T
Department of Biotechnology, Royal Institute of Technology, Center for Structural Biochemistry, Novum, Sweden.
FEBS Lett. 2001 Jan 26;489(1):67-70. doi: 10.1016/s0014-5793(00)02438-8.
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 (15)N NMR relaxation measurements are all consistent with a monomer-dimer equilibrium with a dissociation constant on the order of 60 microM. 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.
布鲁顿酪氨酸激酶(Btk)的SH3结构域之前是含有富含脯氨酸序列的Tec同源(TH)区域。我们研究了一个包含Btk SH3结构域和TH区域富含脯氨酸序列(PRR-SH3)的蛋白质片段。分子间核磁共振交叉弛豫测量、凝胶渗透色谱图、用富含脯氨酸肽进行的滴定以及(15)N核磁共振弛豫测量均与解离常数约为60 microM的单体-二聚体平衡一致。分子间相互作用至少部分涉及TH区域中的富含脯氨酸序列。Btk PRR-SH3的这种行为可能对Btk的功能作用有影响。