Schutt C E, Lindberg U, Myslik J, Strauss N
MRC Laboratory of Molecular Biology, Cambridge, England.
J Mol Biol. 1989 Oct 20;209(4):735-46. doi: 10.1016/0022-2836(89)90603-7.
Analysis of profilin: actin crystals reveals an extensive intermolecular network, rather than a discrete "monomeric complex", comprising stacked actin ribbons held in place by columns of profilin molecules, wedged in between neighboring actin subunits and running perpendicular to the ribbons. Comparison with data from electron microscopy, X-ray diffraction, spectroscopy, and biochemistry of actin suggests that a simple transformation relates the ribbon to f-actin. The crystals exhibit unusual polymorphic properties, which strengthens the view that movements within the actin monomer are important for force generation.
肌动蛋白晶体的分析揭示了一个广泛的分子间网络，而非离散的“单体复合物”，该网络由肌动蛋白条带堆叠而成，肌动蛋白结合蛋白分子柱将其固定在位，这些分子柱楔入相邻的肌动蛋白亚基之间并垂直于条带排列。与来自电子显微镜、X射线衍射、光谱学以及肌动蛋白生物化学的数据进行比较表明，一种简单的转变将条带与丝状肌动蛋白联系起来。这些晶体表现出不同寻常的多晶型特性，这强化了如下观点：肌动蛋白单体内部的运动对于力的产生很重要。
