螺旋线圈
中间灯丝
结晶学
蛋白质丝
中间丝蛋白
原肌球蛋白
微管
细胞骨架
二聚体
超螺旋
肌动蛋白
生物物理学
拉明
蛋白质数据库
蛋白质结构
化学
生物
核心
肌球蛋白
DNA
细胞生物学
DNA超螺旋
生物化学
细胞
有机化学
DNA复制
作者
Dmytro Guzenko,A.A. Chernyatina,S.V. Strelkov
出处
期刊:Sub-cellular biochemistry
日期:2017-01-01
卷期号:: 151-170
被引量:27
标识
DOI:10.1007/978-3-319-49674-0_6
摘要
Intermediate filaments (IFs), together with microtubules and actin microfilaments, are the three main cytoskeletal components in metazoan cells. IFs are formed by a distinct protein family, which is made up of 70 members in humans. Most IF proteins are tissue- or organelle-specific, which includes lamins, the IF proteins of the nucleus. The building block of IFs is an elongated dimer, which consists of a central α-helical 'rod' domain flanked by flexible N- and C-terminal domains. The conserved rod domain is the 'signature feature' of the IF family. Bioinformatics analysis reveals that the rod domain of all IF proteins contains three α-helical segments of largely conserved length, interconnected by linkers. Moreover, there is a conserved pattern of hydrophobic repeats within each segment, which includes heptads and hendecads. This defines the presence of both left-handed and almost parallel coiled-coil regions along the rod length. Using X-ray crystallography on multiple overlapping fragments of IF proteins, the atomic structure of the nearly complete rod domain has been determined. Here, we discuss some specific challenges of this procedure, such as crystallization and diffraction data phasing by molecular replacement. Further insights into the structure of the coiled coil and the terminal domains have been obtained using electron paramagnetic resonance measurements on the full-length protein, with spin labels attached at specific positions. This atomic resolution information, as well as further interesting findings, such as the variation of the coiled-coil stability along the rod length, provide clues towards interpreting the data on IF assembly, collected by a range of methods. However, a full description of this process at the molecular level is not yet at hand.
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