1H, 13C and 15N resonance assignments for a chemokine receptor-binding domain of FROUNT, a cytoplasmic regulator of chemotaxis
1H, 13C and 15N resonance assignments for a chemokine receptor-binding domain of FROUNT, a cytoplasmic regulator of chemotaxis
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FROUNT（一种趋化性细胞质调节因子）的趋化因子受体结合结构域的 1H、13C 和 15N 共振分配
DOI：
10.1007/s12104-018-9819-2
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发表时间：
2018
影响因子：
0.9
通讯作者：
Terasawa Hiroaki
中科院分区：
文献类型：
--
作者：
Yoshinaga Sosuke;Ishida Norihito;Tsuji Tatsuichiro;Sonoda Akihiro;Yunoki Kaori;Takeda Mitsuhiro;Toda Etsuko;Terashima Yuya;Matsushima Kouji;Terasawa Hiroaki
FROUNT 是一种细胞质蛋白，与 CCR2 和 CCR5 趋化因子受体的近膜 C 端区域 (Pro-Cs) 相互作用。 FROUNT 与趋化因子受体之间的相互作用在炎症免疫细胞的迁移中发挥重要作用。因此，FROUNT是炎症性疾病的潜在药物靶点。然而，FROUNT 和趋化因子受体之间相互作用的结构基础仍有待阐明。我们之前鉴定了FROUNT的C端区域（残基532-656）作为负责Pro-C结合的结构域，称为趋化因子受体结合域（CRBD），然后构建了其突变体，带有L538E/P612S突变，具有改善的NMR谱质量，称为CRBD_LEPS。我们现在报告 CRBD_LEPS 的主链和侧链 1H、13C 和 15N 共振分配。 CRBD_LEPS的NMR信号在1H-15N HSQC谱上分散良好，强度均匀，因此几乎所有的主链和侧链共振都被分配。该分配信息为 NMR 研究 CRBD_LEPS 在溶液中的三维结构及其与趋化因子受体的相互作用提供了基础。
FROUNT is a cytoplasmic protein that interacts with the membrane-proximal C-terminal regions (Pro-Cs) of the CCR2 and CCR5 chemokine receptors. The interactions between FROUNT and the chemokine receptors play an important role in the migration of inflammatory immune cells. Therefore, FROUNT is a potential drug target for inflammatory diseases. However, the structural basis of the interactions between FROUNT and the chemokine receptors remains to be elucidated. We previously identified the C-terminal region (residues 532–656) of FROUNT as the structural domain responsible for the Pro-C binding, referred to as the chemokine receptor-binding domain (CRBD), and then constructed its mutant, bearing L538E/P612S mutations, with improved NMR spectral quality, referred to as CRBD_LEPS. We now report the main-chain and side-chain1H,13C, and15N resonance assignments of CRBD_LEPS. The NMR signals of CRBD_LEPS were well dispersed and their intensities were uniform on the1H–15N HSQC spectrum, and thus almost all of the main-chain and side-chain resonances were assigned. This assignment information provides the foundation for NMR studies of the three-dimensional structure of CRBD_LEPS in solution and its interactions with chemokine receptors.