Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
FEBS Lett. 2012 Feb 17;586(4):314-8. doi: 10.1016/j.febslet.2012.01.007. Epub 2012 Jan 16.
We present here the crystal structures of human lamin B1 globular tail domain and coiled 2B domain, which adopt similar folds to Ig-like domain and coiled-coil domain of lamin A, respectively. Despite the overall similarity, we found an extra intermolecular disulfide bond in the lamin B1 coil 2B domain, which does not exist in lamin A/C. In addition, the structural analysis indicates that interactions at the lamin B1 homodimer interface are quite different from those of lamin A/C. Thus our research not only reveals the diversely formed homodimers among lamin family members, but also sheds light on understanding the important roles of lamin B1 in forming the nuclear lamina matrix.
我们在此呈现了人源核纤层蛋白 B1 球状尾部结构域和卷曲 2B 结构域的晶体结构，它们分别采用了类似于核纤层蛋白 A 的免疫球蛋白样结构域和卷曲螺旋结构域的折叠方式。尽管整体上相似，但我们发现核纤层蛋白 B1 卷曲 2B 结构域中有一个额外的分子间二硫键，而在核纤层蛋白 A/C 中则不存在。此外，结构分析表明，核纤层蛋白 B1 同源二聚体界面的相互作用与核纤层蛋白 A/C 的完全不同。因此，我们的研究不仅揭示了核纤层蛋白家族成员之间形成的多样化同源二聚体，还为理解核纤层蛋白 B1 在形成核层基质中的重要作用提供了线索。
