This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1n6j

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:46, 2 December 2020

Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2

Structural highlights

1n6j is a 5 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	MEF2B OR XMEF2 (HUMAN), CABIN1 OR KIAA0330 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] [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

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 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^[3]

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

References

↑ Sun L, Youn HD, Loh C, Stolow M, He W, Liu JO. Cabin 1, a negative regulator for calcineurin signaling in T lymphocytes. Immunity. 1998 Jun;8(6):703-11. PMID:9655484
↑ Tagami H, Ray-Gallet D, Almouzni G, Nakatani Y. Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell. 2004 Jan 9;116(1):51-61. PMID:14718166
↑ Han A, Pan F, Stroud JC, Youn HD, Liu JO, Chen L. Sequence-specific recruitment of transcriptional co-repressor Cabin1 by myocyte enhancer factor-2. Nature. 2003 Apr 17;422(6933):730-4. PMID:12700764 doi:10.1038/nature01555

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n6j"

@@ Line 1: / Line 1: @@
 ==Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2==
-<StructureSection load='1n6j' size='340' side='right' caption='[[1n6j]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N6J FirstGlance]. <br>
+<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>
 </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>
-<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=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'>[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>
 </table>
 == Function ==
@@ Line 13: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n6/1n6j_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n6/1n6j_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 28: @@
 </div>
 <div class="pdbe-citations 1n6j" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Myocyte enhancer factor 2|Myocyte enhancer factor 2]]
 == References ==
 <references/>
@@ Line 33: / Line 36: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Chen, L]]
 [[Category: Han, A]]

1n6j

From Proteopedia

Revision as of 08:46, 2 December 2020

Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox