Undecided membrane proteins insert in random topologies. Up, down and sideways: it does not really matter.
Undecided membrane proteins insert in random topologies. Up, down and sideways: it does not really matter.
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DOI:
10.1016/j.tibs.2012.02.006
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发表时间:
2012-06
影响因子:
13.8
通讯作者:
Schuldiner, Shimon
中科院分区:
文献类型:
--
作者:
Schuldiner, Shimon
It is usually assumed that to ensure proper function, membrane proteins must be inserted in a unique topology. However, a number of dimeric small multidrug transporters can function in the membrane in various topologies. Thus, the dimers can be a random mixture of NiCi (N- and C-termini facing the cell cytoplasm) and NoCo (N- and C-termini facing the outside) orientation. In addition, the dimer functions whether the two protomers are parallel (N- and C-termini of both protomers on the same side of the membrane) or anti-parallel (N- and C-termini of each protomer on opposite sides of the membrane). This unique phenomenon provides strong support for a simple mechanism of transport where the directionality is determined solely by the driving force
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