Department of Chemistry, University of Wisconsin-Whitewater, Whitewater, Wisconsin 53190, United States.
Biochemistry. 2012 Jan 24;51(3):733-5. doi: 10.1021/bi201601k. Epub 2012 Jan 17.
CCL21 is a human chemokine that recruits normal immune cells and metastasizing tumor cells to lymph nodes through activation of the G protein-coupled receptor CCR7. The CCL21 structure solved by NMR contains a conserved chemokine domain followed by an extended, unstructured C-terminus that is not typical of most other chemokines. A sedimentation equilibrium study showed CCL21 to be monomeric. Chemical shift mapping indicates that the CCR7 N-terminus binds to the N-loop and third β-strand of CCL21's chemokine domain. Details of CCL21-receptor recognition may enable structure-based drug discovery of novel antimetastatic agents.
CCL21 是一种人类趋化因子，通过激活 G 蛋白偶联受体 CCR7 将正常免疫细胞和转移的肿瘤细胞募集到淋巴结。通过 NMR 解析的 CCL21 结构包含一个保守的趋化因子结构域，其后是一个延伸的、无结构的 C 末端，这在大多数其他趋化因子中并不典型。沉降平衡研究表明 CCL21 是单体。化学位移映射表明 CCR7 N 末端结合到 CCL21 的趋化因子结构域的 N 环和第三个 β 链。CCL21-受体识别的细节可能使基于结构的新型抗转移药物发现成为可能。
