6c9l: Difference between revisions
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<StructureSection load='6c9l' size='340' side='right' caption='[[6c9l]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='6c9l' size='340' side='right' caption='[[6c9l]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6c9l]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C9L FirstGlance]. <br> | <table><tr><td colspan='2'>[[6c9l]] is a 6 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=6C9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C9L FirstGlance]. <br> | ||
</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=6c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9l OCA], [http://pdbe.org/6c9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c9l RCSB], [http://www.ebi.ac.uk/pdbsum/6c9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9l ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MEF2B, XMEF2 ([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=6c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9l OCA], [http://pdbe.org/6c9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c9l RCSB], [http://www.ebi.ac.uk/pdbsum/6c9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9l ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[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. | [[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. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The myocyte enhancer factor 2 (MEF2) family of transcription factors plays important roles in developmental processes and adaptive responses. Although MEF2 proteins are known to bind DNA in the nucleus to regulate specific gene expression, there are reports that show that MEF2 also functions in the cytoplasm. Previous structural studies of MEF2 focused exclusively on DNA-bound MEF2 with and without various corepressors or coactivators. While these studies have established a comprehensive structural model of DNA recognition and cofactor recruitment by MEF2, the structure of MEF2 not bound to DNA, which include cytoplasmic MEF2 and free MEF2 in the nucleus, is unknown. Here we determined the structure of the MADS-box/MEF2 domain of MEF2B without DNA nor cofactor. The Apo structure of MEF2B reveals a largely preformed DNA binding interface that may be important for recognizing the shape of DNA from the minor groove side. In addition, our structure also reveals that the C-terminal helix of the MEF2-specific domain could flip up to bind to the hydrophobic groove that serves as the binding sites of MEF2 transcription cofactors. These observations shed new insights into DNA binding and cofactor interaction by MEF2 proteins. | |||
Crystal Structure of Apo MEF2B Reveals New Insights in DNA Binding and Cofactor Interaction.,Lei X, Shi H, Kou Y, Rajashekar N, Wu F, Sen C, Xu J, Chen L Biochemistry. 2018 Jul 17;57(28):4047-4051. doi: 10.1021/acs.biochem.8b00439., Epub 2018 Jul 5. PMID:29944822<ref>PMID:29944822</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6c9l" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Chen, L]] | [[Category: Chen, L]] | ||
[[Category: Lei, X]] | [[Category: Lei, X]] | ||
Revision as of 12:43, 18 July 2018
MEF2B Apo Protein StructureMEF2B Apo Protein Structure
Structural highlights
Function[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. Publication Abstract from PubMedThe myocyte enhancer factor 2 (MEF2) family of transcription factors plays important roles in developmental processes and adaptive responses. Although MEF2 proteins are known to bind DNA in the nucleus to regulate specific gene expression, there are reports that show that MEF2 also functions in the cytoplasm. Previous structural studies of MEF2 focused exclusively on DNA-bound MEF2 with and without various corepressors or coactivators. While these studies have established a comprehensive structural model of DNA recognition and cofactor recruitment by MEF2, the structure of MEF2 not bound to DNA, which include cytoplasmic MEF2 and free MEF2 in the nucleus, is unknown. Here we determined the structure of the MADS-box/MEF2 domain of MEF2B without DNA nor cofactor. The Apo structure of MEF2B reveals a largely preformed DNA binding interface that may be important for recognizing the shape of DNA from the minor groove side. In addition, our structure also reveals that the C-terminal helix of the MEF2-specific domain could flip up to bind to the hydrophobic groove that serves as the binding sites of MEF2 transcription cofactors. These observations shed new insights into DNA binding and cofactor interaction by MEF2 proteins. Crystal Structure of Apo MEF2B Reveals New Insights in DNA Binding and Cofactor Interaction.,Lei X, Shi H, Kou Y, Rajashekar N, Wu F, Sen C, Xu J, Chen L Biochemistry. 2018 Jul 17;57(28):4047-4051. doi: 10.1021/acs.biochem.8b00439., Epub 2018 Jul 5. PMID:29944822[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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