Gonçalves Rui Pedro, Buzhysnskyy Nikolay, Scheuring Simon
Laboratory of Cell Biophysics, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
J Bioenerg Biomembr. 2008 Jun;40(3):133-8. doi: 10.1007/s10863-008-9141-2.
The Voltage Dependent Anion Channel (VDAC) is the most abundant protein in the outer membrane of mitochondria. This strategic localization puts it at the heart of a great number of phenomena. Its recent implication in apoptosis is an example of the major importance of this protein and has created a surge of interest in VDAC. There is no atomic-resolution structure allowing a better understanding of the function of VDAC, so alternative techniques to X-ray diffraction have been used to study VDAC. Here we discuss structural models from folding predictions and review data acquired by Atomic Force Microscopy (AFM) imaging that allowed to observe VDAC's structure and supramolecular organization in the mitochondrial outer membrane.
电压依赖性阴离子通道(VDAC)是线粒体外膜中含量最丰富的蛋白质。这种关键的定位使其处于众多现象的核心位置。它最近在细胞凋亡中的作用就是该蛋白质重要性的一个例证,并引发了对VDAC的大量研究兴趣。目前尚无原子分辨率结构能更好地理解VDAC的功能,因此已采用X射线衍射之外的其他技术来研究VDAC。在此,我们讨论基于折叠预测的结构模型,并回顾通过原子力显微镜(AFM)成像获得的数据,这些数据使我们能够观察到VDAC在线粒体外膜中的结构和超分子组织。