Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1

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.Structured summary of protein interactionsLamin-B and Lamin-Bbind by x-ray crystallography (View interaction)

► Crystal structures of the human lamin B1 coil 2B and tail domains are presented.
► These two domains in lamin B1 adopt conserved folds to those of lamin A/C.
► An intermolecular disulfide bond is revealed in the coil 2B coiled-coil homodimer.
► Different structure features distinguish lamin B1 from other nuclear lamins.