Domain movement in gelsolin: A calcium-activated switch
Domain movement in gelsolin: A calcium-activated switch
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DOI：
10.1126/science.286.5446.1939
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发表时间：
1999-12-03
期刊：
影响因子：
56.9
通讯作者：
Choe, S
中科院分区：
文献类型：
--
作者：
Robinson, RC;Mejillano, M;Choe, S
肌动蛋白结合蛋白凝胶在生长因子信号传导、细胞凋亡、细胞分裂和细胞运动过程中参与肌动蛋白骨架的重塑。与肌动蛋白复合物的凝胶中羧基末端一半（G4-G6）的3.4埃x射线结构揭示了凝胶活化的基础。钙结合诱导构象重排，其中结构域G6相对于G4和G5翻转并翻译约40埃。结构重组撕裂了G4和G6连续的beta片核。这暴露了G4上的肌动蛋白结合位点，使肌动蛋白丝的切断和封盖得以进行。
The actin-binding protein gelsolin is involved in remodeling the actin cytoskeleton during growth-factor signaling, apoptosis, cytokinesis, and cell movement. Calcium-activated gelsolin severs and caps actin filaments, The 3.4 angstrom x-ray structure of the carboxyl-terminal half of gelsolin (G4-G6) in complex with actin reveals the basis for gelsolin activation. Calcium binding induces a conformational rearrangement in which domain G6 is flipped over and translated by about 40 angstroms relative to G4 and G5. The structural reorganization tears apart the continuous beta sheet core of G4 and G6. This exposes the actin-binding site on G4, enabling severing and capping of actin filaments to proceed.