Structural Symmetry in Membrane Proteins.
Structural Symmetry in Membrane Proteins.
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DOI:
10.1146/annurev-biophys-051013-023008
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发表时间:
2015
影响因子:
12.4
通讯作者:
Forrest LR
中科院分区:
文献类型:
--
作者:
Forrest LR
Symmetry is a common feature among natural systems, including protein structures. A strong propensity towards symmetric architectures has long been recognized for water-soluble proteins, and rationalized from an evolutionary standpoint. Proteins residing in cellular membranes, however, have traditionally been less amenable to structural studies, and thus the prevalence and significance of symmetry in this important class of molecules is not as well understood. In the past two decades great strides have been made in this area, providing exciting insights into the range of architectures adopted by membrane proteins. These structural studies have revealed a similarly strong bias toward symmetric arrangements, often unexpected, despite the restrictions imposed by the membrane environment on the possible symmetry groups. Moreover, membrane proteins disproportionately contain internal structural repeats resulting from duplication and fusion of smaller segments. Here, the types and origins of symmetry in membrane proteins are discussed, along with the implications for their function.
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