Mannella Carmen A, Kinnally Kathleen W
Resource for Visualization of Biological Complexity, Wadsworth Center, Albany, NY 12201-0509, USA.
J Bioenerg Biomembr. 2008 Jun;40(3):149-55. doi: 10.1007/s10863-008-9143-0.
There is excellent agreement between the electrophysiological properties and the structure of the mitochondrial outer membrane protein, VDAC, ex vivo. However, the inference that the well-defined canonical "open" state of the VDAC pore is the normal physiological state of the channel in vivo is being challenged by several lines of evidence. Knowing the atomic structure of the detergent solubilized protein, a long sought after goal, will not be sufficient to understand the functioning of this channel protein. In addition, detailed information about VDAC's topology in the outer membrane of intact mitochondria, and the structural changes that it undergoes in response to different stimuli in the cell will be needed to define its physiological functions and regulation.
在线粒体外膜蛋白电压依赖性阴离子通道（VDAC）的电生理特性与结构之间，在体外存在高度一致性。然而，VDAC孔道明确的典型“开放”状态是该通道在体内的正常生理状态这一推断，正受到多方面证据的挑战。了解去污剂溶解蛋白的原子结构这一长期追求的目标，对于理解这种通道蛋白的功能并不足够。此外，还需要关于VDAC在完整线粒体外膜中的拓扑结构，以及它在细胞内对不同刺激所经历的结构变化的详细信息，以确定其生理功能和调节机制。
