User:Benjamin Elliott/Crystal Structure of the Bromodomain-PHD Finger Module of Human Transcriptional Co-Activator CBP in complex with Acetylated Histone 4 Peptide (H4K20ac)

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== Function ==
== Function ==
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Bromodomains, in general, function as acetyl-lysine binding domains to regulate gene transcription in chromatin. This particular bromodomain of CBP binds with relatively high specificity to Lys20-acetylated histone H4 (H4K20), though this preference is not well understood.
== Disease ==
== Disease ==
== Relevance ==
== Relevance ==
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Bromodomains have become a popular target for their role in human disease since they recognize an epigenetic tag.
== Structural highlights ==
== Structural highlights ==

Revision as of 22:53, 4 October 2017

Your Heading Here (maybe something like 'Structure')

Caption for this structure

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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Benjamin Elliott

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