1jei

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==Overview==
==Overview==
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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.
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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.
==Disease==
==Disease==
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[[Category: emerin nucleus membrane domain dystrophy]]
[[Category: emerin nucleus membrane domain dystrophy]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:45 2008''

Revision as of 11:21, 21 February 2008


1jei

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LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN EMERIN

Contents

Overview

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.

Disease

Known diseases associated with this structure: Emery-Dreifuss muscular dystrophy OMIM:[300384]

About this Structure

1JEI is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy., Wolff N, Gilquin B, Courchay K, Callebaut I, Worman HJ, Zinn-Justin S, FEBS Lett. 2001 Jul 20;501(2-3):171-6. PMID:11470279

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