3aqa | pdb_00003aqa
From Proteopedia
Crystal structure of the human BRD2 BD1 bromodomain in complex with a BRD2-interactive compound, BIC1
Function
[BRD2_HUMAN] May play a role in spermatogenesis or folliculogenesis (By similarity). Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly.[1]
About this Structure
3aqa is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Ito T, Umehara T, Sasaki K, Nakamura Y, Nishino N, Terada T, Shirouzu M, Padmanabhan B, Yokoyama S, Ito A, Yoshida M. Real-Time Imaging of Histone H4K12-Specific Acetylation Determines the Modes of Action of Histone Deacetylase and Bromodomain Inhibitors. Chem Biol. 2011 Apr 22;18(4):495-507. PMID:21513886 doi:10.1016/j.chembiol.2011.02.009
- ↑ LeRoy G, Rickards B, Flint SJ. The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription. Mol Cell. 2008 Apr 11;30(1):51-60. doi: 10.1016/j.molcel.2008.01.018. PMID:18406326 doi:10.1016/j.molcel.2008.01.018
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Homo sapiens
- Nakamura, Y.
- Padmanabhan, B.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Shirouzu, M.
- Terada, T.
- Umehara, T.
- Yokoyama, S.
- Acetyl-lysine recognition
- Acetylated histone h4
- Helical bundle
- Nucleus
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomic
- Transcription-transcription inhibitor complex
