Ampe C, Vandekerckhove J
Laboratory of Physiological Chemistry, State University Ghent, Belgium.
Semin Cell Biol. 1994 Jun;5(3):175-82. doi: 10.1006/scel.1994.1022.
The recent elucidation of the three-dimensional structure of gelsolin segment 1 and profilin provides new insights on how these proteins recognize actin. Although the picture is still incomplete and not all biochemical data are consolidated, the results offer clues on how these proteins exert their effect on actin and how they may modulate the cytoskeleton dynamics. Binding studies on the villin head piece, thymosin beta 4 and mutants of both peptides allowed to identify critical residues important for actin binding and give the first picture of new actin binding interfaces. The interface of the modelled actomyosin complex is also briefly discussed.
最近对凝溶胶蛋白片段1和丝切蛋白三维结构的阐明，为这些蛋白质如何识别肌动蛋白提供了新的见解。尽管情况仍不完整，并非所有生化数据都已整合，但这些结果为这些蛋白质如何对肌动蛋白发挥作用以及如何调节细胞骨架动力学提供了线索。对绒毛蛋白头部片段、胸腺素β4以及这两种肽的突变体的结合研究，使得能够识别对肌动蛋白结合至关重要的关键残基，并给出了新的肌动蛋白结合界面的首张图片。还简要讨论了模拟的肌动球蛋白复合物的界面。
