Letter to the Editor:: 1H, 13C and 15N backbone resonance assignments of the hyaluronan-binding domain of CD44
Letter to the Editor:: 1H, 13C and 15N backbone resonance assignments of the hyaluronan-binding domain of CD44
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DOI：
10.1023/b:jnmr.0000019465.12250.e0
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发表时间：
2004-05-01
影响因子：
2.7
通讯作者：
Shimada, I
中科院分区：
文献类型：
--
作者：
Takeda, M;Terasawa, H;Shimada, I
CD 44是透明质酸（HA）的主要细胞表面受体，并且CD 44与HA的结合涉及细胞粘附于细胞外基质（ECM）组分和细胞信号传导级联（Lesley et al.，1993; Naor等人，1997年）。CD 44含有一个功能性HA结合结构域（HABD），由具有N-和C-末端延伸的连接模块组成。在几种ECM分子和肿瘤坏死因子刺激基因-6（TSG-6）的蛋白产物中发现了连接模块（Day等人，2002年）。TSG-6连接模块的三维结构和配体结合位点已经通过NMR确定（Kohda等人，1996; Kahmann等人，2000）。除了连接模块，CD 44还需要N-和C-末端的延伸来实现其正确的折叠和功能活性，但没有关于CD 44的结构信息。在这里，我们报告的1H，13 C和15 N骨架共振分配的CD 44 HABD。从本研究中获得的分配将用于阐明HA识别模式的CD 44 HABD的交叉饱和和化学位移扰动实验。
CD44 is the main cell surface receptor for hyaluronic acid (HA), and the binding of CD44 to HA has been implicated in both cell adhesion to the extracellular matrix (ECM) components and cellular signaling cascades (Lesley et al., 1993; Naor et al., 1997). CD44 contains a functional HA-binding domain (HABD) composed of a Link module with N-and C-terminal extensions. Link modules are found in several ECM molecules and the protein product of tumor necrosis factor-stimulated gene-6 (TSG-6)(Day et al., 2002). The three-dimensional structure and ligand-binding site of the TSG-6 Link module have already been determined by NMR (Kohda et al., 1996; Kahmann et al., 2000). In addition to the Link module, CD44 requires N-and C-terminal extensions for its proper folding and the functional activity, but no structural information about CD44 is available. Here we report the 1H, 13C and 15N backbone resonance assignments for the CD44 HABD. The assignments obtained from the present study will be used to elucidate the HA-recognition mode of CD44 HABD by cross-saturation and chemical shift perturbation experiments.