NMR INVESTIGATION OF BINDING DOMAIN OF CD2BP2: T CELL SIGNAL TRANSDUCTION

本研究项目的目的是确定核磁共振溶液 胞内蛋白CD2BP2结合区的结构 并对CD2BP2与胞浆的相互作用进行了表征 CD2细胞表面受体的结构域。这种互动是至关重要的 用于CD2介导的IL-2在T细胞激活时的产生。 1998年，CD2BP2分离结合域的三维结构 并与CD2胞浆结构域结合部位为 通过化学位移分析绘制。同核和同核的数据 UP750核磁共振记录的异核编辑NOESY谱 光谱仪是获得高分辨率结构的关键 CD2BP2的结合域。这个域的结构 揭示了一种识别富含脯氨酸序列的新折叠 很可能代表了一个尚未定义的家族的第一个成员 蛋白质结构域。未来的实验将集中在 复合体中CD2BP2结合域及其识别序列 在CD2胞质结构域内。在高磁环境下记录的数据 对于这个问题的调查，菲尔兹肯定是不可或缺的。 有趣的分子相互作用。

The aim of this research project is to determine the NMR solution structure of the binding domain of the intracellular protein CD2BP2 and to characterize the interaction of CD2BP2 with the cytoplasmic domain of the CD2 cell surface receptor. This interaction is critical for CD2 mediated interleukin-2 production upon T cell activation. During 1998, the 3D-structure of the isolated binding domain of CD2BP2 was solved and the binding site for the CD2 cytoplasmic domain was mapped by chemical shift analysis. The data of the homonuclear and the heteronuclear edited NOESY spectra recorded at the UP750 NMR spectrometer were critical for obtaining a high resolution structure of the binding domain of CD2BP2. The structure of this domain revealed a novel fold for the recognition of proline-rich sequences and probably represents a first member of a yet undefined family of protein domains. Future experiments will focus on the structure of the CD2BP2 binding domain in complex with its recognition sequence within the CD2 cytoplasmic domain. Data recorded at high magnetic fields will certainly be indispensable for the investigation of this interesting molecular interaction.