2odg

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m (Protected "2odg" [edit=sysop:move=sysop])
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[[Image:2odg.png|left|200px]]
 
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{{STRUCTURE_2odg| PDB=2odg | SCENE= }}
{{STRUCTURE_2odg| PDB=2odg | SCENE= }}
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===Complex of barrier-to-autointegration factor and LEM-domain of emerin===
===Complex of barrier-to-autointegration factor and LEM-domain of emerin===
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{{ABSTRACT_PUBMED_17355960}}
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{{ABSTRACT_PUBMED_17355960}}
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==Disease==
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[[http://www.uniprot.org/uniprot/BAF_HUMAN BAF_HUMAN]] Defects in BANF1 are the cause of Nestor-Guillermo progeria syndrome (NGPS) [MIM:[http://omim.org/entry/614008 614008]]. NGPS is an atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognatia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies.<ref>PMID:21549337</ref> [[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>
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==Function==
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[[http://www.uniprot.org/uniprot/BAF_HUMAN BAF_HUMAN]] Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. 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.<ref>PMID:11005805</ref><ref>PMID:12163470</ref><ref>PMID:16680152</ref> [[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>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:017355960</ref><references group="xtra"/>
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<ref group="xtra">PMID:017355960</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Cai, M.]]
[[Category: Cai, M.]]

Revision as of 10:10, 24 March 2013

Template:STRUCTURE 2odg

Contents

Complex of barrier-to-autointegration factor and LEM-domain of emerin

Template:ABSTRACT PUBMED 17355960

Disease

[BAF_HUMAN] Defects in BANF1 are the cause of Nestor-Guillermo progeria syndrome (NGPS) [MIM:614008]. NGPS is an atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognatia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies.[1] [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.[2][3][4][5]

Function

[BAF_HUMAN] Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. 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.[6][7][8] [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.[9][10][11][12][13]

About this Structure

2odg is a 3 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • 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. ↑ Puente XS, Quesada V, Osorio FG, Cabanillas R, Cadinanos J, Fraile JM, Ordonez GR, Puente DA, Gutierrez-Fernandez A, Fanjul-Fernandez M, Levy N, Freije JM, Lopez-Otin C. Exome sequencing and functional analysis identifies BANF1 mutation as the cause of a hereditary progeroid syndrome. Am J Hum Genet. 2011 May 13;88(5):650-6. doi: 10.1016/j.ajhg.2011.04.010. Epub, 2011 May 5. PMID:21549337 doi:10.1016/j.ajhg.2011.04.010
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ Harris D, Engelman A. Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro. J Biol Chem. 2000 Dec 15;275(50):39671-7. PMID:11005805 doi:10.1074/jbc.M002626200
  7. ↑ Segura-Totten M, Kowalski AK, Craigie R, Wilson KL. Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. J Cell Biol. 2002 Aug 5;158(3):475-85. Epub 2002 Aug 5. PMID:12163470 doi:10.1083/jcb.200202019
  8. ↑ 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
  9. ↑ 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
  10. ↑ 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
  11. ↑ 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
  12. ↑ 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
  13. ↑ 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

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