Human emerin is an inner nuclear membrane protein involved in the response of the nucleus to mechanical stress. It contributes to the physical connection between the cytoskeleton and the nucleoskeleton. It is also involved in chromatin organization. Its N-terminal region is nucleoplasmic and comprises a globular LEM domain from residue 1 to residue 43. The three-dimensional structure of this LEM domain in complex with the chromatin BAF protein was solved from NMR data. Apart from the LEM domain, the nucleoplasmic region of emerin, from residue 44 to residue 221, is predicted to be intrinsically disordered. Mutations in this region impair binding to several emerin partners as lamin A, actin or HDAC3. However the molecular details of these recognition defects are unknown. Here we report 1H, 15N, 13CO, 13Cα and 13Cβ NMR chemical shift assignments of the emerin fragment from residue 67 to residue 170, which is sufficient for nuclear localization and involved in lamin A binding. Chemical shift analysis confirms that this fragment is intrinsically disordered in 0 and 8 M urea.
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We thank the French Association against Myopathies (AFM) (research Grant No. 17243 to S.Z.J. and fellowship No. 18159 to C.S.) and the Foundation for Medical Research (FRM) (Grant. FDT20140931008 to I.H.) for providing financial support to this project. We also thank the Leibniz-Institut für Molekular Pharmakologie (FMP) for access to the NMR facility.
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