Summary for 3UMN
| Entry DOI | 10.2210/pdb3umn/pdb |
| Descriptor | Lamin-B1 (2 entities in total) |
| Functional Keywords | structural genomics consortium, sgc, ig-like domain, intermediate filament, lipoprotein, membrane, nucleus, structural protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side: P20700 |
| Total number of polymer chains | 3 |
| Total formula weight | 40280.93 |
| Authors | Xu, C.,Bian, C.B.,Amaya, M.F.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2011-11-14, release date: 2011-11-30, Last modification date: 2024-02-28) |
| Primary citation | Ruan, J.,Xu, C.,Bian, C.,Lam, R.,Wang, J.P.,Kania, J.,Min, J.,Zang, J. Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1. Febs Lett., 586:314-318, 2012 Cited by PubMed Abstract: 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. PubMed: 22265972DOI: 10.1016/j.febslet.2012.01.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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