Bromodomain-containing protein

From Proteopedia

Revision as of 11:33, 27 May 2018

spinqualitylabelsall models Human bromodomain-containing protein 4 bromodomain 1 complex with inhibitor and ethylene glycol (PDB code 3p5o) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Bromodomain-containing proteins (BRD) are active as histone acetyltransferase, chromatin remodeling and transcriptional mediation. The bromodomain is a ca. 110 amino acid long sequence which recognizes acetylated lysine residues which are found in the C-terminal of histones[1]. For detalis on BRD3 see Human bromodomain containing protein 3 Disease Dysfunction of BRD is involved in cancer, inflammation, obesity and multiple sclerosis[2]. BRD4 translocations are detected in NUT midline carcinoma and a variety of BRD4 inhibitors are clinically tested at the present[3]. Structural highlights [4]. Water molecules are shown as red spheres.

3D Structures of bromodomain-containing protein

Updated on 27-May-2018

References

1. ↑ Zeng L, Zhou MM. Bromodomain: an acetyl-lysine binding domain. FEBS Lett. 2002 Feb 20;513(1):124-8. PMID:11911891
2. ↑ Belkina AC, Denis GV. BET domain co-regulators in obesity, inflammation and cancer. Nat Rev Cancer. 2012 Jun 22;12(7):465-77. doi: 10.1038/nrc3256. PMID:22722403 doi:http://dx.doi.org/10.1038/nrc3256
3. ↑ French CA. Demystified molecular pathology of NUT midline carcinomas. J Clin Pathol. 2010 Jun;63(6):492-6. doi: 10.1136/jcp.2007.052902. Epub 2008 Jun , 13. PMID:18552174 doi:http://dx.doi.org/10.1136/jcp.2007.052902
4. ↑ French CA. Demystified molecular pathology of NUT midline carcinomas. J Clin Pathol. 2010 Jun;63(6):492-6. doi: 10.1136/jcp.2007.052902. Epub 2008 Jun , 13. PMID:18552174 doi:http://dx.doi.org/10.1136/jcp.2007.052902