Fukuzawa Atsushi, Idowu Seraphina, Gautel Mathias
The Randall Division of Cell and Molecular Biophysics and The Cardiovascular Division, New Hunt's House, King's College London, SE1 1UL, London, United Kingdom.
J Muscle Res Cell Motil. 2005;26(6-8):427-34. doi: 10.1007/s10974-005-9025-6.
The complete gene giant muscle protein obscurin, a modular protein composed largely of tandem Ig-domains, GDP/GTP exchange factor domains (GEF) for small G-proteins, and differentially spliced kinase domains, was analysed. The splice donor and acceptor sites of the 117 exons give important clues for potential splice pathways. The fusion of the conventional obscurin A, containing only the GEF domain, and obscurin B, fusing into the 3' kinase exons, was experimentally confirmed and analysed. The linker between the two kinases contains multiple predicted phosphorylation sites, as well as a predicted NFX zinc finger domain. Both kinases show only weak homology to either myosin light chain kinases or other giant muscle protein kinases, suggesting that they are functionally distinct.
对完整的巨大肌肉蛋白 obscurin 基因进行了分析，该蛋白是一种模块化蛋白，主要由串联免疫球蛋白结构域、小 G 蛋白的 GDP/GTP 交换因子结构域（GEF）和可变剪接的激酶结构域组成。117 个外显子的剪接供体和受体位点为潜在的剪接途径提供了重要线索。仅包含 GEF 结构域的传统 obscurin A 与融合到 3' 激酶外显子的 obscurin B 的融合通过实验得到证实并进行了分析。两种激酶之间的连接区包含多个预测的磷酸化位点，以及一个预测的 NFX 锌指结构域。两种激酶与肌球蛋白轻链激酶或其他巨大肌肉蛋白激酶的同源性都很弱，这表明它们在功能上是不同的。
