CXCR3型
CXCL10型
趋化因子受体
CCR3
细胞生物学
受体
化学
生物物理学
C-C趋化因子受体6型
趋化因子
趋化因子受体
生物化学
生物
作者
Valerie Booth,David W. Keizer,Monique B. Kamphuis,Ian Clark‐Lewis,Brian D. Sykes
出处
期刊:Biochemistry
[American Chemical Society]
日期:2002-07-23
卷期号:41 (33): 10418-10425
被引量:141
摘要
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.
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