1JEI
LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN EMERIN
Summary for 1JEI
| Entry DOI | 10.2210/pdb1jei/pdb |
| Related | 1H9E 1H9F |
| NMR Information | BMRB: 5074 |
| Descriptor | EMERIN (1 entity in total) |
| Functional Keywords | emerin nucleus membrane domain dystrophy, membrane protein |
| Cellular location | Nucleus inner membrane; Single-pass membrane protein; Nucleoplasmic side: P50402 |
| Total number of polymer chains | 1 |
| Total formula weight | 6237.95 |
| Authors | Wolff, N.,Gilquin, B.,Courchay, K.,Callebaut, I.,Zinn-Justin, S. (deposition date: 2001-06-18, release date: 2001-07-04, Last modification date: 2024-05-29) |
| Primary citation | Wolff, N.,Gilquin, B.,Courchay, K.,Callebaut, I.,Worman, H.J.,Zinn-Justin, S. Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy FEBS LETT., 501:171-176, 2001 Cited by PubMed Abstract: Like Duchenne and Becker muscular dystrophies, Emery-Dreifuss muscular dystrophy (EDMD) is characterized by myopathic and cardiomyopathic abnormalities. EDMD has the particularity of being linked to mutations in nuclear proteins. The X-linked form of EDMD is caused by mutations in the emerin gene, whereas autosomal dominant EDMD is caused by mutations in the lamin A/C gene. Emerin colocalizes with lamin A/C in interphase cells, and binds in vitro to lamin A/C. Recent work suggests that lamin A/C might serve as a receptor for emerin. We have undertaken a structural analysis of emerin, and in particular of its N-terminal domain, which is comprised in the emerin segment critical for binding to lamin A/C. We show that region 2-54 of emerin adopts the LEM fold. This fold was originally described in the two N-terminal domains of another inner nuclear membrane protein called lamina-associated protein 2 (LAP2). The existence of a conserved solvent-exposed surface on the LEM domains of LAP2 and emerin is discussed, as well as the nature of a possible common target. PubMed: 11470279DOI: 10.1016/S0014-5793(01)02649-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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