View source for 1jei


==LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN EMERIN==
<StructureSection load='1jei' size='340' side='right'caption='[[1jei]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jei]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JEI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jei OCA], [https://pdbe.org/1jei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jei RCSB], [https://www.ebi.ac.uk/pdbsum/1jei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jei ProSAT]</span></td></tr>
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== Disease ==
[https://www.uniprot.org/uniprot/EMD_HUMAN EMD_HUMAN] Defects in EMD are the cause of Emery-Dreifuss muscular dystrophy type 1 (EDMD1) [MIM:[https://omim.org/entry/310300 310300]. A degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.<ref>PMID:15328537</ref> <ref>PMID:15009215</ref> <ref>PMID:10323252</ref> <ref>PMID:11587540</ref> 
== Function ==
[https://www.uniprot.org/uniprot/EMD_HUMAN EMD_HUMAN] Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C.<ref>PMID:15328537</ref> <ref>PMID:16858403</ref> <ref>PMID:16680152</ref> <ref>PMID:17785515</ref> <ref>PMID:19323649</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/je/1jei_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jei ConSurf].
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:11470279</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Callebaut I]]
[[Category: Courchay K]]
[[Category: Gilquin B]]
[[Category: Wolff N]]
[[Category: Zinn-Justin S]]