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CD 2BP 2结合域的结构 并表征CD 2BP 2与细胞质的相互作用 CD 2细胞表面受体的结构域。 这种互动是至关重要的 T细胞活化后CD 2介导的白细胞介素-2产生。 在1998年期间，CD 2BP 2的分离的结合结构域的3D结构 的结合位点，并为CD 2胞质结构域的结合位点， 通过化学位移分析绘制。 数据的homecycle和 在UP 750 NMR处记录的异源编辑的NOESY光谱 光谱仪对于获得高分辨率结构是关键 CD 2BP 2的结合域。 此域的结构 揭示了一个新的折叠识别脯氨酸丰富的序列 可能代表了一个尚未定义的 蛋白质结构域。 未来的实验将集中在 与其识别序列复合的CD 2BP 2结合结构域 在CD 2胞质结构域内。 在高磁场下记录数据 这些领域肯定是调查这一问题所不可或缺的。 有趣的分子间相互作用

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.