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| | ==LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN LAP2== | | ==LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN LAP2== |
| - | <StructureSection load='1h9f' size='340' side='right'caption='[[1h9f]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1h9f' size='340' side='right'caption='[[1h9f]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h9f]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H9F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h9f]] 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=1H9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H9F FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h9e|1h9e]]</div></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9f OCA], [https://pdbe.org/1h9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h9f RCSB], [https://www.ebi.ac.uk/pdbsum/1h9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h9f ProSAT]</span></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=1h9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9f OCA], [https://pdbe.org/1h9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h9f RCSB], [https://www.ebi.ac.uk/pdbsum/1h9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h9f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/LAP2A_HUMAN LAP2A_HUMAN]] Defects in TMPO are the cause of cardiomyopathy dilated type 1T (CMD1T) [MIM:[https://omim.org/entry/613740 613740]]. A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:16247757</ref>
| + | [https://www.uniprot.org/uniprot/LAP2A_HUMAN LAP2A_HUMAN] Defects in TMPO are the cause of cardiomyopathy dilated type 1T (CMD1T) [MIM:[https://omim.org/entry/613740 613740]. A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:16247757</ref> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LAP2A_HUMAN LAP2A_HUMAN]] May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1. TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.
| + | [https://www.uniprot.org/uniprot/LAP2A_HUMAN LAP2A_HUMAN] May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1. TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Callebaut, I]] | + | [[Category: Callebaut I]] |
| - | [[Category: Courchay, K]] | + | [[Category: Courchay K]] |
| - | [[Category: Gilquin, B]] | + | [[Category: Gilquin B]] |
| - | [[Category: Laguri, C]] | + | [[Category: Laguri C]] |
| - | [[Category: Romi-Lebrun, R]] | + | [[Category: Romi-Lebrun R]] |
| - | [[Category: Wolff, N]] | + | [[Category: Wolff N]] |
| - | [[Category: Worman, H J]] | + | [[Category: Worman HJ]] |
| - | [[Category: Zinn-Justin, S]] | + | [[Category: Zinn-Justin S]] |
| - | [[Category: Emerin]]
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| - | [[Category: Inner nuclear membrane protein]]
| + | |
| - | [[Category: Lamina-associated polypeptide]]
| + | |
| - | [[Category: Lem domain]]
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| - | [[Category: Membrane protein]]
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| Structural highlights
Disease
LAP2A_HUMAN Defects in TMPO are the cause of cardiomyopathy dilated type 1T (CMD1T) [MIM:613740. A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.[1]
Function
LAP2A_HUMAN May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1. TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.
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
BACKGROUND: Integral membrane proteins of the inner nuclear membrane are involved in chromatin organization and postmitotic reassembly of the nucleus. The discovery that mutations in the gene encoding emerin causes X-linked Emery-Dreifuss muscular dystrophy has enhanced interest in such proteins. A common structural domain of 50 residues, called the LEM domain, has been identified in emerin MAN1, and lamina-associated polypeptide (LAP) 2. In particular, all LAP2 isoforms share an N-terminal segment composed of such a LEM domain that is connected to a highly divergent LEM-like domain by a linker that is probably unstructured. RESULTS: We have determined the three-dimensional structures of the LEM and LEM-like domains of LAP2 using nuclear magnetic resonance and molecular modeling. Both domains adopt the same fold, mainly composed of two large parallel alpha helices. CONCLUSIONS: The structural LEM motif is found in human inner nuclear membrane proteins and in protein-protein interaction domains from bacterial multienzyme complexes. This suggests that LEM and LEM-like domains are protein-protein interaction domains. A region conserved in all LEM domains, at the surface of helix 2, could mediate interaction between LEM domains and a common protein partner.
Structural characterization of the LEM motif common to three human inner nuclear membrane proteins.,Laguri C, Gilquin B, Wolff N, Romi-Lebrun R, Courchay K, Callebaut I, Worman HJ, Zinn-Justin S Structure. 2001 Jun;9(6):503-11. PMID:11435115[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Taylor MR, Slavov D, Gajewski A, Vlcek S, Ku L, Fain PR, Carniel E, Di Lenarda A, Sinagra G, Boucek MM, Cavanaugh J, Graw SL, Ruegg P, Feiger J, Zhu X, Ferguson DA, Bristow MR, Gotzmann J, Foisner R, Mestroni L. Thymopoietin (lamina-associated polypeptide 2) gene mutation associated with dilated cardiomyopathy. Hum Mutat. 2005 Dec;26(6):566-74. PMID:16247757 doi:10.1002/humu.20250
- ↑ Laguri C, Gilquin B, Wolff N, Romi-Lebrun R, Courchay K, Callebaut I, Worman HJ, Zinn-Justin S. Structural characterization of the LEM motif common to three human inner nuclear membrane proteins. Structure. 2001 Jun;9(6):503-11. PMID:11435115
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