6bz1

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==MEF2 Chimera D83V mutant/DNA complex==
==MEF2 Chimera D83V mutant/DNA complex==
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<StructureSection load='6bz1' size='340' side='right' caption='[[6bz1]], [[Resolution|resolution]] 2.97&Aring;' scene=''>
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<StructureSection load='6bz1' size='340' side='right'caption='[[6bz1]], [[Resolution|resolution]] 2.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6bz1]] is a 8 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=6BZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BZ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6bz1]] is a 8 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=6BZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BZ1 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MEF2A, MEF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.97&#8491;</td></tr>
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<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=6bz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bz1 OCA], [http://pdbe.org/6bz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bz1 RCSB], [http://www.ebi.ac.uk/pdbsum/6bz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bz1 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bz1 OCA], [https://pdbe.org/6bz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bz1 RCSB], [https://www.ebi.ac.uk/pdbsum/6bz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bz1 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/MEF2A_HUMAN MEF2A_HUMAN]] Defects in MEF2A are a cause of coronary artery disease, autosomal dominant, type 1 (ADCAD1) [MIM:[http://omim.org/entry/608320 608320]]. A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction.
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[https://www.uniprot.org/uniprot/MEF2A_HUMAN MEF2A_HUMAN] Defects in MEF2A are a cause of coronary artery disease, autosomal dominant, type 1 (ADCAD1) [MIM:[https://omim.org/entry/608320 608320]. A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MEF2A_HUMAN MEF2A_HUMAN]] Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation.<ref>PMID:9858528</ref> <ref>PMID:11904443</ref> <ref>PMID:12691662</ref> <ref>PMID:15834131</ref> <ref>PMID:16563226</ref> <ref>PMID:16371476</ref> <ref>PMID:16484498</ref>
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[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.[https://www.uniprot.org/uniprot/MEF2A_HUMAN MEF2A_HUMAN] Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation.<ref>PMID:9858528</ref> <ref>PMID:11904443</ref> <ref>PMID:12691662</ref> <ref>PMID:15834131</ref> <ref>PMID:16563226</ref> <ref>PMID:16371476</ref> <ref>PMID:16484498</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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MEF2B is a major target of somatic mutations in non-Hodgkin lymphoma. Most of these mutations are non-synonymous substitutions of surface residues in the MADS-box/MEF2 domain. Among them, D83V is the most frequent mutation found in tumor cells. The link between this hotspot mutation and cancer is not well understood. Here we show that the D83V mutation induces a dramatic alpha-helix to beta-strand switch in the MEF2 domain. Located in an alpha-helix region rich in beta-branched residues, the D83V mutation not only removes the extensive helix stabilization interactions but also introduces an additional beta-branched residue that further shifts the conformation equilibrium from alpha-helix to beta-strand. Cross-database analyses of cancer mutations and chameleon sequences revealed a number of well-known cancer targets harboring beta-strand favoring mutations in chameleon alpha-helices, suggesting a commonality of such conformational switch in certain cancers and a new factor to consider when stratifying the rapidly expanding cancer mutation data.
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The cancer mutation D83V induces an alpha-helix to beta-strand conformation switch in MEF2B.,Lei X, Kou Y, Fu Y, Rajashekar N, Shi H, Wu F, Xu J, Luo Y, Chen L J Mol Biol. 2018 Feb 22. pii: S0022-2836(18)30085-8. doi:, 10.1016/j.jmb.2018.02.012. PMID:29477338<ref>PMID:29477338</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6bz1" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Chen, L]]
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[[Category: Large Structures]]
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[[Category: Lei, X]]
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[[Category: Chen L]]
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[[Category: Conformation switch]]
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[[Category: Lei X]]
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[[Category: D83v mutant]]
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[[Category: Mef2]]
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[[Category: Transcription factor]]
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[[Category: Transcription-dna complex]]
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Current revision

MEF2 Chimera D83V mutant/DNA complex

PDB ID 6bz1

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