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Journal Articles Structure Year : 2001

Structural Characterization of the LEM Motif Common to Three Human Inner Nuclear Membrane Proteins

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Abstract

Background: Integral membrane proteins of the inner nuclear membrane are involved in chromatin organization and postmitotic reassembly of the nucleus. The discovery that mutations in the gene encoding emerin causes X-linked Emery-Dreifuss muscular dystrophy has enhanced interest in such proteins. A common structural domain of 50 residues, called the LEM domain, has been identified in emerin MAN1, and lamina-associated polypeptide (LAP) 2. In particular, all LAP2 isoforms share an N-terminal segment composed of such a LEM domain that is connected to a highly divergent LEM-like domain by a linker that is probably unstructured. Results: We have determined the three-dimensional structures of the LEM and LEM-like domains of LAP2 using nuclear magnetic resonance and molecular modeling. Both domains adopt the same fold, mainly composed of two large parallel alpha helices. Conclusions: The structural LEM motif is found in human inner nuclear membrane proteins and in protein-protein interaction domains from bacterial multienzyme complexes. This suggests that LEM and LEM-like domains are protein-protein interaction domains. A region conserved in all LEM domains, at the surface of helix 2, could mediate interaction between LEM domains and a common protein partner.

Dates and versions

pasteur-02884048 , version 1 (29-06-2020)

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Cédric Laguri, Bernard Gilquin, Nicolas Wolff, Régine Romi-Lebrun, Karine Courchay, et al.. Structural Characterization of the LEM Motif Common to Three Human Inner Nuclear Membrane Proteins. Structure, 2001, 9 (6), pp.503-511. ⟨10.1016/s0969-2126(01)00611-6⟩. ⟨pasteur-02884048⟩
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