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神经热素-3和p75NTR对称复合物的晶体结构

Yong Gong¹, Peng Cao, Hong-jun Yu

¹National Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.

|July 4, 2008

概括

神经营养素 (NTs) 通过与p75神经营养素受体 (p75(NTR)) 结合来调节神经元的生存和功能. 这项研究揭示了NT-3与糖化p75(NTR形成了一个对称的2:2复合体,表明本地激活状态.

科学领域:

神经科学是一个神经科学.
分子生物学分子生物学
结构生物学结构生物学

背景情况:

神经营养素 (NTs) 对于神经元的生存,分化和维护至关重要.
NTs与p75神经热素受体 (p75(NTR)) 和氨酸激酶受体 (Trks) 相互作用.
通过NTs激活p75 (NTR) 的机制,特别是受体二分化,仍在争论中.

研究的目的:

阐明神经热素-3 (NT-3) 结合p75(NTR) ECTODOMAIN的结构基础.
为了比较 glycosylated p75(NTR) 复合物的结构与以前报告的脱糖化形式.
为了确定NT-p75 (NTR) 相互作用的本源静脉测量.

主要方法:

进行X射线晶体学以确定NT-3/p75 (NTR) 复合体的2.6 Å分辨率结构.
生物化学实验,以评估溶液中的结合性静脉测量.
糖化和脱糖化复合物的比较结构分析.

主要成果:

晶体结构显示NT-3形成一个同极体,它对称地结合了两种糖化p75的分子,形成一个2:2复合体.
相比之下,神经生长因子 (NGF) 与脱糖化p75 (NTR) 结合形成了一个不对称的2:1复合体.
生物化学试验证实了NT-3和NGF与溶液中的p75 (NTR) 的2:2胆量计,表明2:1复合物来自脱糖化.

结论:

对称的 2:2 NT-3/p75(NTR) 复合体代表了p75(NTR) 激活的原始状态.
这一发现为NT-p75 (NTR) 识别和信号提供了一个结构模型.
结果提供了关于p75 (NTR) 和Trk受体通路之间的相互作用的见解.

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