2odc

From Proteopedia

(Difference between revisions)

Current revision

LEM-domain of the nuclear envelope protein emerin

Structural highlights

2odc is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

EMD_HUMAN Defects in EMD are the cause of Emery-Dreifuss muscular dystrophy type 1 (EDMD1) [MIM: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.^[1] ^[2] ^[3] ^[4]

Function

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.^[5] ^[6] ^[7] ^[8] ^[9]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The barrier-to-autointegration factor BAF binds to the LEM domain (Em(LEM)) of the nuclear envelope protein emerin and plays an essential role in the nuclear architecture of metazoan cells. In addition, the BAF(2) dimer bridges and compacts double-stranded DNA nonspecifically via two symmetry-related DNA binding sites. In this article we present biophysical and structural studies on a complex of BAF(2) and Em(LEM). Light scattering, analytical ultracentrifugation, and NMR indicate a stoichiometry of one molecule of Em(LEM) bound per BAF(2) dimer. The equilibrium dissociation constant (K(d)) for the interaction of the BAF(2) dimer and Em(LEM), determined by isothermal titration calorimetry, is 0.59 +/- 0.03 microm. Z-exchange spectroscopy between corresponding cross-peaks of the magnetically non-equivalent subunits of the BAF(2) dimer in the complex yields a dissociation rate constant of 78 +/- 2s(-1). The solution NMR structure of the BAF(2)-Em(LEM) complex reveals that the LEM and DNA binding sites on BAF(2) are non-overlapping and that both subunits of the BAF(2) dimer contribute approximately equally to the Em(LEM) binding site. The relevance of the implications of the structural and biophysical data on the complex in the context of the interaction between the BAF(2) dimer and Em(LEM) at the nuclear envelope is discussed.

Solution NMR structure of the barrier-to-autointegration factor-Emerin complex.,Cai M, Huang Y, Suh JY, Louis JM, Ghirlando R, Craigie R, Clore GM J Biol Chem. 2007 May 11;282(19):14525-35. Epub 2007 Mar 13. PMID:17355960^[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Holaska JM, Kowalski AK, Wilson KL. Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. PLoS Biol. 2004 Sep;2(9):E231. Epub 2004 Aug 24. PMID:15328537 doi:10.1371/journal.pbio.0020231
↑ Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y. Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy. Eur J Biochem. 2004 Mar;271(5):1035-45. PMID:15009215
↑ Ellis JA, Yates JR, Kendrick-Jones J, Brown CA. Changes at P183 of emerin weaken its protein-protein interactions resulting in X-linked Emery-Dreifuss muscular dystrophy. Hum Genet. 1999 Mar;104(3):262-8. PMID:10323252
↑ Holt I, Clements L, Manilal S, Morris GE. How does a g993t mutation in the emerin gene cause Emery-Dreifuss muscular dystrophy? Biochem Biophys Res Commun. 2001 Oct 12;287(5):1129-33. PMID:11587540 doi:10.1006/bbrc.2001.5708
↑ Holaska JM, Kowalski AK, Wilson KL. Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. PLoS Biol. 2004 Sep;2(9):E231. Epub 2004 Aug 24. PMID:15328537 doi:10.1371/journal.pbio.0020231
↑ Markiewicz E, Tilgner K, Barker N, van de Wetering M, Clevers H, Dorobek M, Hausmanowa-Petrusewicz I, Ramaekers FC, Broers JL, Blankesteijn WM, Salpingidou G, Wilson RG, Ellis JA, Hutchison CJ. The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus. EMBO J. 2006 Jul 26;25(14):3275-85. Epub 2006 Jul 20. PMID:16858403 doi:10.1038/sj.emboj.7601230
↑ Jacque JM, Stevenson M. The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity. Nature. 2006 Jun 1;441(7093):641-5. Epub 2006 May 7. PMID:16680152 doi:10.1038/nature04682
↑ Salpingidou G, Smertenko A, Hausmanowa-Petrucewicz I, Hussey PJ, Hutchison CJ. A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane. J Cell Biol. 2007 Sep 10;178(6):897-904. Epub 2007 Sep 4. PMID:17785515 doi:10.1083/jcb.200702026
↑ Capanni C, Del Coco R, Mattioli E, Camozzi D, Columbaro M, Schena E, Merlini L, Squarzoni S, Maraldi NM, Lattanzi G. Emerin-prelamin A interplay in human fibroblasts. Biol Cell. 2009 Sep;101(9):541-54. doi: 10.1042/BC20080175. PMID:19323649 doi:10.1042/BC20080175
↑ Cai M, Huang Y, Suh JY, Louis JM, Ghirlando R, Craigie R, Clore GM. Solution NMR structure of the barrier-to-autointegration factor-Emerin complex. J Biol Chem. 2007 May 11;282(19):14525-35. Epub 2007 Mar 13. PMID:17355960 doi:10.1074/jbc.M700576200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2odc"

Categories: Homo sapiens | Large Structures | Cai M | Clore GM

@@ Line 1: / Line 1: @@
 ==LEM-domain of the nuclear envelope protein emerin==
-<StructureSection load='2odc' size='340' side='right' caption='[[2odc]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='2odc' size='340' side='right'caption='[[2odc]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2odc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ODC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2odc]] 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=2ODC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ODC FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2odg|2odg]]</td></tr>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EMD, EDMD, STA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2odc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odc OCA], [https://pdbe.org/2odc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2odc RCSB], [https://www.ebi.ac.uk/pdbsum/2odc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2odc ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2odc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odc OCA], [http://pdbe.org/2odc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2odc RCSB], [http://www.ebi.ac.uk/pdbsum/2odc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2odc ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/EMD_HUMAN EMD_HUMAN]] Defects in EMD are the cause of Emery-Dreifuss muscular dystrophy type 1 (EDMD1) [MIM:[http://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>
+[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 ==
-[[http://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>
+[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]]
@@ Line 35: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Cai, M]]
+[[Category: Large Structures]]
-[[Category: Clore, G M]]
+[[Category: Cai M]]
-[[Category: Inner nuclear membrane protein]]
+[[Category: Clore GM]]
-[[Category: Lem-domain multidimensional nmr dipolar coupling]]
-[[Category: Membrane protein]]

2odc

From Proteopedia

Current revision

LEM-domain of the nuclear envelope protein emerin

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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