Rose A, Meier I
Plant Biotechnology Center and Department of Cellular and Molecular Plant Biology, The Ohio State University, 244 Rightmire Hall, 1060 Carmack Road, 43210-1002, Columbus, Ohio 43210-1002, USA.
Cell Mol Life Sci. 2004 Aug;61(16):1996-2009. doi: 10.1007/s00018-004-4039-6.
Long alpha-helical coiled-coil proteins are involved in a variety of organizational and regulatory processes in eukaryotic cells. They provide cables and networks in the cyto- and nucleoskeleton, molecular scaffolds that organize membrane systems, motors, levers, rotating arms and possibly springs. A growing number of human diseases are found to be caused by mutations in long coiled-coil proteins. This review summarizes our current understanding of the multifaceted group of long coiled-coil proteins in the cytoskeleton, nucleus, Golgi and cell division apparatus. The biophysical features of coiled-coil domains provide first clues toward their contribution to the diverse protein functions and promise potential future applications in the area of nanotechnology. Combining the power of fully sequenced genomes and structure prediction algorithms, it is now possible to comprehensively summarize and compare the complete inventory of coiled-coil proteins of different organisms.
长α-螺旋卷曲螺旋蛋白参与真核细胞中的多种组织和调节过程。它们在细胞骨架和核骨架中提供缆线和网络、组织膜系统的分子支架、马达、杠杆、旋转臂以及可能的弹簧。越来越多的人类疾病被发现是由长卷曲螺旋蛋白的突变引起的。本综述总结了我们目前对细胞骨架、细胞核、高尔基体和细胞分裂装置中长卷曲螺旋蛋白这一多面群体的理解。卷曲螺旋结构域的生物物理特征为其对多种蛋白质功能的贡献提供了初步线索，并有望在纳米技术领域得到潜在的未来应用。结合全基因组测序的力量和结构预测算法，现在有可能全面总结和比较不同生物体中卷曲螺旋蛋白的完整清单。
