The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function.
The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function.
复制标题
DOI：
--
复制
发表时间：
1992-02
影响因子：
6.5
通讯作者：
J. Segrest;Martin K. Jones;H. Loof;C. Brouillette;Y. Venkatachalapathi;G. Anantharamaiah
中科院分区：
文献类型：
--
作者：
J. Segrest;Martin K. Jones;H. Loof;C. Brouillette;Y. Venkatachalapathi;G. Anantharamaiah
定点突变和其他基于分子生物学的技术现在可用于探测可交换载脂蛋白中的两亲性α螺旋结构基序。在这里，我们调查了已发表的文献载脂蛋白A-I，A-II，A-IV，C-I，C-II，C-III和E的脂质结合和功能结构域，并比较这些结果与最近开发的计算机方法分析的位置和性能的两亲性螺旋。这种比较表明，有至少三个不同的类的两亲性螺旋（类A，Y和G *）的可交换载脂蛋白，其分布范围内和之间的七个载脂蛋白。这种比较进一步表明，脂质亲和力主要存在于A类两亲性螺旋中（Segrest，J.P.，等，1990年。proteins.第八章：103），并且单个载脂蛋白中A类结构域的结构和/或数量的变化允许从高到低的一系列脂质亲和力。四个α螺旋的位置最近显示在apoE中形成4-螺旋束球状结构（Wilson，C.，等，1991。科学252：1817）与通过我们的计算机分析鉴定的apoE的四个氨基末端G * 类两亲螺旋紧密对应。因此，特别令人感兴趣的是，除apoA-II和C-I外，所有可交换的载脂蛋白都含有G * 类的两亲性螺旋。将讨论可交换载脂蛋白的结构和功能的两亲性螺旋异质性的其他影响。
Site-directed mutagenesis and other molecular biology-based techniques are now available for probing the amphipathic alpha helix structural motif in the exchangeable apolipoproteins. Here we survey the published literature on lipid-binding and functional domains in apolipoproteins A-I, A-II, A-IV, C-I, C-II, C-III, and E and compare these results with recently developed computer methods for analysis of the location and properties of amphipathic helixes. This comparison suggests that there are at least three distinct classes of amphipathic helixes (classes A, Y, and G*) in the exchangeable apolipoproteins whose distribution varies within and between the seven apolipoproteins. This comparison further suggests that lipid affinity resides largely in class A amphipathic helixes (Segrest, J. P., et al. 1990. Proteins. 8: 103) and that variations in structure and/or numbers of class A domains in individual apolipoproteins allow a range of lipid affinities from high to low. The positions of the four alpha helixes recently shown to form a 4-helix bundle globular structure in apoE (Wilson, C., et al. 1991. Science. 252: 1817) correspond closely to the four amino-terminal class G* amphipathic helixes of apoE identified by our computer analysis. It is of particular interest, therefore, that all of the exchangeable apolipoproteins except apoA-II and C-I, contain amphipathic helixes of class G*. Additional implications of amphipathic helix heterogeneity for the structure and function of the exchangeable apolipoproteins will be discussed.