Myocyte enhancer factor 2: Difference between revisions

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Through the structure of this oligomer that was obtained by crystallography, we can see that HDAC9 is kept <scene name='Sandbox_Reserved_1/Binding/3'>relatively far from the genomic DNA </scene> even after MEF2 binding to the chromosome. We can also easily observe a very well <scene name='Sandbox_Reserved_1/Conservation/7'>evolutionary conserved region</scene> near the DNA binding site of MEF2.

Additionally, by looking to the <scene name='Sandbox_Reserved_1/False_dimer/2'>structure</scene> obtained by X-ray crystallography, one could also think that complexes HDAC9/MEF2/DNA dimerize ''in vivo''. During the crystallization process, two complexes were contained in the same asymmetric unit, giving such a false impression. Thus, it is important to emphasize that the biological unit would be composed only by <scene name='Sandbox_Reserved_1/Complex/5'>a monomer of HDAC9, a dimer of MEF2 and a fragment of double strand DNA</scene>.

Additionally, by looking to the <scene name='Sandbox_Reserved_1/False_dimer/2'>structure</scene> obtained by X-ray crystallography, one could also think that complexes HDAC9/MEF2/DNA dimerize ''in vivo''. During the crystallization process, two complexes were contained in the same asymmetric unit, giving such a false impression. Thus, it is important to emphasize that the biological unit would be composed only by <scene name='Sandbox_Reserved_1/Complex/5'>a monomer of HDAC9, a dimer of MEF2 and a fragment of double strand DNA</scene>[http://www.ebi.ac.uk/pdbe/pqs/pqs-bin/macmol.pl?filename=1TQE].

Myocyte enhancer factor 2: Difference between revisions

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Revision as of 02:52, 1 July 2009 view source Ricardo Alchini (talk \| contribs) 4 edits New page: left\|200px {{STRUCTURE_1tqe\| PDB=1tqe \| SCENE= }} =Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure= A biological field that has rece...		Revision as of 02:54, 1 July 2009 view source Ricardo Alchini (talk \| contribs) 4 edits No edit summary Newer edit →
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	Through the structure of this oligomer that was obtained by crystallography, we can see that HDAC9 is kept <scene name='Sandbox_Reserved_1/Binding/3'>relatively far from the genomic DNA </scene> even after MEF2 binding to the chromosome. We can also easily observe a very well <scene name='Sandbox_Reserved_1/Conservation/7'>evolutionary conserved region</scene> near the DNA binding site of MEF2.		Through the structure of this oligomer that was obtained by crystallography, we can see that HDAC9 is kept <scene name='Sandbox_Reserved_1/Binding/3'>relatively far from the genomic DNA </scene> even after MEF2 binding to the chromosome. We can also easily observe a very well <scene name='Sandbox_Reserved_1/Conservation/7'>evolutionary conserved region</scene> near the DNA binding site of MEF2.

	Additionally, by looking to the <scene name='Sandbox_Reserved_1/False_dimer/2'>structure</scene> obtained by X-ray crystallography, one could also think that complexes HDAC9/MEF2/DNA dimerize ''in vivo''. During the crystallization process, two complexes were contained in the same asymmetric unit, giving such a false impression. Thus, it is important to emphasize that the biological unit would be composed only by <scene name='Sandbox_Reserved_1/Complex/5'>a monomer of HDAC9, a dimer of MEF2 and a fragment of double strand DNA</scene>.		Additionally, by looking to the <scene name='Sandbox_Reserved_1/False_dimer/2'>structure</scene> obtained by X-ray crystallography, one could also think that complexes HDAC9/MEF2/DNA dimerize ''in vivo''. During the crystallization process, two complexes were contained in the same asymmetric unit, giving such a false impression. Thus, it is important to emphasize that the biological unit would be composed only by <scene name='Sandbox_Reserved_1/Complex/5'>a monomer of HDAC9, a dimer of MEF2 and a fragment of double strand DNA</scene>[http://www.ebi.ac.uk/pdbe/pqs/pqs-bin/macmol.pl?filename=1TQE].