User:Elizabeth Cook/Sandbox 1: Difference between revisions

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The full-length CECR2 is composed of an N-terminus DDT domain (DNA-binding homeobox and different transcription factors), an AT-hook, and a bromodomain.<ref>DOI: 10.1074/jbc.RA120.014598 </ref><ref>DOI: 10.1387/ijdb.092933jc</ref>The DDT and the AT-hook domain bind DNA, while the bromodomain recognizes acetylated lysine.<ref>DOI: 10.1093/nar/26.19.4413.</ref><ref>DOI: 10.1111/jipb.12069  From NLM Medline.</ref><ref>DOI: 10.1016/j.cell.2012.02.013</ref>
The full-length CECR2 is composed of an N-terminus DDT domain (DNA-binding homeobox and different transcription factors), an AT-hook, and a bromodomain.<ref>DOI: 10.1074/jbc.RA120.014598 </ref><ref>DOI: 10.1387/ijdb.092933jc</ref>The DDT and the AT-hook domain bind DNA, while the bromodomain recognizes acetylated lysine.<ref>DOI: 10.1093/nar/26.19.4413.</ref><ref>DOI: 10.1111/jipb.12069  From NLM Medline.</ref><ref>DOI: 10.1016/j.cell.2012.02.013</ref>
== Sequential and Structural Conservation ==
[[Image:Msa.jpg |300px|]]
CECR2 has multiple 100% sequence alignment matches across various species, indicative of its importance and how well it has been conserved, particularly the bromodomain. This provides insight into the essential biological roles performed by CECR2 that have remained critical across millions of years of evolution. The high similarity across different species suggest that even small changes could be harmful, meaning CECR2 is fundamental to processes like DNA replication and gene regulation.
[[Image:Conserved_cecr2.jpg |300px|]]
In addition to being sequentially conserved, CECR2 is also structurally conserved, particularly within the binding pocket. Conservation of structure is indicative of the structural properties being crucial for CECR2’s function and that the mechanism in which it functions is critical across species.


== Bromodomains ==
== Bromodomains ==