Specificity and promiscuity in membrane helix interactions
Specificity and promiscuity in membrane helix interactions
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DOI：
10.1016/0014-5793(94)00467-6
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发表时间：
1994-06
期刊：
影响因子：
3.5
通讯作者：
M. Lemmon;D. Engelman
中科院分区：
文献类型：
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作者：
M. Lemmon;D. Engelman
许多完整膜蛋白的跨膜部分由一个或多个跨膜α-螺旋组成，它们在热力学上是独立稳定的。这些跨膜α-螺旋之间的并排相互作用在这些整合膜蛋白及其复合物的折叠和组装中是重要的。在考虑这些螺旋-螺旋相互作用对膜蛋白折叠和寡聚化的贡献时，应该认识到能量学和特异性之间的区别。对脂质双层内跨膜螺旋缔合的能量学的许多贡献将是相对非特异性的，包括由电荷-电荷相互作用和脂质包装效应产生的那些。然而，跨膜α-螺旋缔合的特异性（和部分能量）似乎主要依赖于特定螺旋的动态可达状态之间的详细立体化学拟合。在某些情况下，这些相互作用部分由辅基介导。
The membrane-spanning portions of many integral membrane proteins consist of one or a number of transmembrane α-helices, which are expected to be independently stable on thermodynamic grounds. Side-by-side interactions between these transmembrane α-helices are important in the folding and assembly of such integral membrane proteins and their complexes. In considering the contribution of these helix–helix interactions to membrane protein folding and oligomerization, a distinction between the energetics and specificity should be recognized. A number of contributions to the energetics of transmembrane helix association within the lipid bilayer will be relatively non-specific, including those resulting from charge–charge interactions and lipid–packing effects. Specificity (and part of the energy) in transmembrane α-helix association, however, appears to rely mainly upon a detailed stereochemical fit between sets of dynamically accessible states of particular helices. In some cases, these interactions are mediated in part by prosthetic groups.