1n6j: Difference between revisions

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 <StructureSection load='1n6j' size='340' side='right'caption='[[1n6j]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n6j]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N6J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n6j]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N6J FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MEF2B OR XMEF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CABIN1 OR KIAA0330 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6j OCA], [http://pdbe.org/1n6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n6j RCSB], [http://www.ebi.ac.uk/pdbsum/1n6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n6j 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=1n6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6j OCA], [https://pdbe.org/1n6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n6j RCSB], [https://www.ebi.ac.uk/pdbsum/1n6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n6j ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CABIN_HUMAN CABIN_HUMAN]] May be required for replication-independent chromatin assembly. May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. Inhibition of activated calcineurin is dependent on both PKC and calcium signals.<ref>PMID:9655484</ref> <ref>PMID:14718166</ref>  [[http://www.uniprot.org/uniprot/MEF2B_HUMAN MEF2B_HUMAN]] Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription.
+[https://www.uniprot.org/uniprot/MEF2B_HUMAN MEF2B_HUMAN] Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1n6j ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The myocyte enhancer factor-2 (MEF2) family of transcription factors has important roles in the development and function of T cells, neuronal cells and muscle cells. MEF2 is capable of repressing or activating transcription by association with a variety of co-repressors or co-activators in a calcium-dependent manner. Transcriptional repression by MEF2 has attracted particular attention because of its potential role in hypertrophic responses of cardiomyocytes. Several MEF2 co-repressors, such as Cabin1/Cain and class II histone deacetylases (HDACs), have been identified. However, the molecular mechanism of their recruitment to specific promoters by MEF2 remains largely unknown. Here we report a crystal structure of the MADS-box/MEF2S domain of human MEF2B bound to a motif of the transcriptional co-repressor Cabin1 and DNA at 2.2 A resolution. The crystal structure reveals a stably folded MEF2S domain on the surface of the MADS box. Cabin1 adopts an amphipathic alpha-helix to bind a hydrophobic groove on the MEF2S domain, forming a triple-helical interaction. Our studies of the ternary Cabin1/MEF2/DNA complex show a general mechanism by which MEF2 recruits transcriptional co-repressor Cabin1 and class II HDACs to specific DNA sites.
-Sequence-specific recruitment of transcriptional co-repressor Cabin1 by myocyte enhancer factor-2.,Han A, Pan F, Stroud JC, Youn HD, Liu JO, Chen L Nature. 2003 Apr 17;422(6933):730-4. PMID:12700764<ref>PMID:12700764</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1n6j" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Myocyte enhancer factor 2|Myocyte enhancer factor 2]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Chen, L]]
+[[Category: Chen L]]
-[[Category: Han, A]]
+[[Category: Han A]]
-[[Category: Liu, J O]]
+[[Category: Liu JO]]
-[[Category: Pan, F]]
+[[Category: Pan F]]
-[[Category: Stroud, J C]]
+[[Category: Stroud JC]]
-[[Category: Youn, H D]]
+[[Category: Youn HD]]
-[[Category: Histone deacetylase]]
-[[Category: Mads-box]]
-[[Category: Protein-dna complex]]
-[[Category: Transcription-dna complex]]