Bromodomain-containing protein: Difference between revisions

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'''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<ref>PMID:11911891</ref>.
'''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<ref>PMID:11911891</ref>.
*'''BRD1''' is essential for normal brain development<ref>PMID:35941107</ref>.
   
   
For detalis on BRD3 see [[Human bromodomain containing protein 3]]
For detalis on BRD3 see [[Human bromodomain containing protein 3]]

Revision as of 13:23, 30 May 2024

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].

  • BRD1 is essential for normal brain development[2].

For detalis on BRD3 see Human bromodomain containing protein 3

Disease

Dysfunction of BRD is involved in cancer, inflammation, obesity and multiple sclerosis[3]. BRD4 translocations are detected in NUT midline carcinoma and a variety of BRD4 inhibitors are clinically tested at the present[4].

Structural highlights

[5]. Water molecules are shown as red spheres.


3D Structures of bromodomain-containing protein

Bromodomain-containing protein 3D structures


Human bromodomain-containing protein 4 bromodomain 1 complex with inhibitor and ethylene glycol (PDB code 3p5o)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Zeng L, Zhou MM. Bromodomain: an acetyl-lysine binding domain. FEBS Lett. 2002 Feb 20;513(1):124-8. PMID:11911891
  2. ↑ Paternoster V, Cömert C, Kirk LS, la Cour SH, Fryland T, Fernandez-Guerra P, Stougaard M, Nyengaard JR, Qvist P, Bross P, Børglum AD, Christensen JH. The psychiatric risk gene BRD1 modulates mitochondrial bioenergetics by transcriptional regulation. Transl Psychiatry. 2022 Aug 8;12(1):319. PMID:35941107 doi:10.1038/s41398-022-02053-2
  3. ↑ 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
  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
  5. ↑ 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

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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