The CXCR3 binding chemokine IP-10/CXCL10: Structure and receptor interactions
The CXCR3 binding chemokine IP-10/CXCL10: Structure and receptor interactions
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DOI：
10.1021/bi026020q
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发表时间：
2002-08-20
期刊：
影响因子：
2.9
通讯作者：
Sykes, BD
中科院分区：
文献类型：
--
作者：
Booth, V;Keizer, DW;Sykes, BD
IP-10的结构通过NMR光谱解析，并且代表针对受体CXCR 3的激动剂类别的第一个结构。CXCR 3结合趋化因子在其结合来自CC和CXC类趋化因子受体的受体的能力方面是独特的。鉴定了IP-10的一个不寻常的结构特征，这可能为IP-10结合CXCR 3和CCR 3的能力提供了基础。与CXCR 3的N-末端相互作用的IP-10的表面通过监测添加CXCR 3 N-末端肽后IP-10的NMR谱的变化来确定。这些研究表明，相互作用涉及IP-10的N-环和40 s-环区域形成的疏水裂缝，类似于对其他趋化因子如IL-8观察到的相互作用表面。观察到由IP-10的N-末端和IP-10的30 s-环形成的疏水裂缝组成的另外的相互作用区域。
The structure of IP-10 was solved by NMR spectroscopy and represents the first structure from the class of agonists toward the receptor CXCR3. CXCR3 binding chemokines are unique in their ability to bind receptors from both the CC and CXC classes of chemokine receptors. An unusual structural feature of IP-10 was identified that may provide the basis for the ability of IP-10 to bind both CXCR3 and CCR3. The surface of IP-10 that interacts with the N-terminus of CXCR3 was defined by monitoring changes in the NMR spectrum of IP-10 upon addition of a CXCR3 N-terminal peptide. These studies indicated that the interaction involves a hydrophobic cleft, formed by the N-loop and 40s-loop region of IP-10, similar to the interaction surface observed for other chemokines such as IL-8. An additional region of interaction was observed that consists of a hydrophobic cleft formed by the N-terminus of IP-10 and 30s-loop of IP-10.