CALCIUM-SENSITIVE NONMUSCLE ALPHA-ACTININ CONTAINS EF-HAND STRUCTURES AND HIGHLY CONSERVED REGIONS
CALCIUM-SENSITIVE NONMUSCLE ALPHA-ACTININ CONTAINS EF-HAND STRUCTURES AND HIGHLY CONSERVED REGIONS
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DOI：
10.1016/0014-5793(87)80962-6
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发表时间：
1987-09-14
期刊：
影响因子：
3.5
通讯作者：
SCHLEICHER, M
中科院分区：
文献类型：
--
作者：
NOEGEL, A;WITKE, W;SCHLEICHER, M
黏菌盘状网柄菌（Dictyosteelium discoideum）的F-肌动蛋白交联分子α-辅肌动蛋白（α-actinin）在C-末端具有两个特征性的EF-手形结构。钙结合环包含所有必需的配位氧，并且最有可能形成严格钙调节的非肌肉α-辅肌动蛋白的钙敏感性的结构基础。此外，该序列在该分子的N-末端位点与鸡成纤维细胞α-辅肌动蛋白具有高度同源性。这段氨基酸似乎在进化过程中基本保持不变，可能代表肌动蛋白结合位点。这一发现使我们提出了一个模型的抑制作用的Ca 2+对非肌肉α-辅肌动蛋白。
The F-actin crosslinking molecule α-actinin from the slime mouldDictyostelium discoideumcarries two characteristics EF-hand structures at the C-terminus. The calcium-binding loops contain all necessary liganding oxygens and most likely form the structural basis for the calcium sensitivity of strictly calcium-regulated non-muscle α-actinins. Furthermore, the sequence exhibits at the N-terminal site of the molecule a high degree of homology to chicken fibroblast α-actinin. This stretch of amino acids appears to have remained essentially constant during evolution and might represent the actin-binding site. The findings have led us to propose a model for the inhibitory action of Ca2+on non-muscle α-actinins.