INTERACTION BETWEEN PROTEINS LOCALIZED IN MEMBRANES
INTERACTION BETWEEN PROTEINS LOCALIZED IN MEMBRANES
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DOI：
10.1073/pnas.83.17.6258
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发表时间：
1986-09-01
影响因子：
11.1
通讯作者：
METZGER, H
中科院分区：
文献类型：
--
作者：
GRASBERGER, B;MINTON, AP;METZGER, H
我们提出了一个概念框架，用于评估膜中蛋白质自缔合的影响，由于（i）在高浓度（排除体积效应）和（ii）反应物种的高浓度和预取向状态的其他蛋白质的存在。我们已经计算了这种影响的大小，使用合理的值的蛋白质在膜中的浓度，蛋白质的倾斜和垂直移动的程度，以及它们的尺寸。与在实验现实的体积中自由翻滚的单体的关联相比，我们计算出仅这些因素就可以增加形成二聚体106倍的可能性，并且形成三聚体和更高的低聚物的可能性大许多数量级。我们讨论了我们的计算的实验操作的膜蛋白，生物合成组装的多亚基膜蛋白和形成膜损伤的外源性蛋白质的组件，和激活的细胞事件引起的膜受体与自己或与其他膜蛋白的相互作用的影响。
We present a conceptual framework for evaluating the effect on the self-association of proteins in membranes due to (i) the presence of other proteins at high concentrations (excluded volume effect) and (ii) the high concentration and preoriented state of the reaction species. We have calculated the magnitude of such effects using plausible values for the concentrations of proteins in membranes, for the degree to which proteins may tilt and move vertically, and for their dimensions. Compared to the association of monomers tumbling freely in an experimentally realistic volume, we calculate that these factors alone can increase the likelihood of forming dimers 106-fold and of forming trimers and higher oligomers many orders of magnitude greater. We discuss the implications of our calculations for experimental manipulations of membrane proteins, for biosynthetic assembly of multisubunit membrane proteins and formation of membrane lesions by assemblies of exogenous proteins, and for the activation of cellular events induced by the interaction of membrane receptors with themselves or with other membrane proteins.