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首页> 外文期刊>Nature structural biology >The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger
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The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger

机译：载脂蛋白A-I的C末端结构域包含脂质敏感的构象触发器

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摘要

Exchangeable apolipoproteins can convert between lipid-free and lipid-associated states. The C-terminal domain of human apolipoprotein A-I ( apoA-I) plays a role in both lipid binding and self-association. Site-directed spin-label electron paramagnetic resonance spectroscopy was used to examine the structure of the apoA-I C terminus in lipid-free and lipid-associated states. Nitroxide spin-labels positioned at defined locations throughout the C terminus were used to define discrete secondary structural elements. Magnetic interactions between probes localized at positions 163, 217 and 226 in singly and doubly labeled apoA-I gave inter-and intramolecular distance information, providing a basis for mapping apoA-I tertiary and quaternary structure. Spectra of apoA-I in reconstituted HDL revealed a lipid-induced transition of defined random coils and - strands into - helices. This conformational switch is analogous to triggered events in viral fusion proteins and may serve as a means to overcome the energy barriers of lipid sequestration, a critical step in cholesterol efflux and HDL assembly. [References: 35]
机译：可交换的载脂蛋白可以在无脂质状态和脂质相关状态之间转换。人载脂蛋白A-1（apoA-I）的C末端结构域在脂质结合和自我缔合中均起作用。使用定点自旋标记电子顺磁共振光谱法检查无脂质和脂质相关状态下apoA-I C末端的结构。位于整个C末端定义位置的一氧化氮自旋标记用于定义离散的二级结构元素。位于单标记和双标记的apoA-I中位于位置163、217和226的探针之间的磁相互作用提供了分子间和分子内的距离信息，为绘制apoA-I三级和四级结构提供了基础。重构的HDL中apoA-I的光谱揭示了脂质诱导的确定的随机线圈和-链到-螺旋的过渡。这种构象转换类似于病毒融合蛋白中的触发事件，并且可以作为克服脂质螯合的能量屏障的手段，脂质屏障是胆固醇外排和HDL组装的关键步骤。 [参考：35]

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