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Bromodomain-containing protein: Difference between revisions

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<StructureSection load='4bw2' size='340' side='right' caption='Human bromodomain-containing protein 4 bromodomain 1 complex with inhibitor (PDB code [[4bw2]])' scene=''>
<StructureSection load='' size='350' side='right' caption='Human bromodomain-containing protein 4 bromodomain 1 complex with inhibitor and ethylene glycol (PDB code [[3p5o]])' scene='72/724778/Cv/1'>
== Function ==
== 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.
'''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>.
<ref>PMID:21638687</ref> to the rescue.
*'''BRD1''' is essential for normal brain development<ref>PMID:35941107</ref>.
For detalis on BRD3 see [[Human bromodomain containing protein 3]]
*'''BRD2''' promotes spatial mixing and compartmentalisation of chromatin<ref>PMID:35410381</ref>.  
*'''BRD3''' and '''BRD4''' regulate skeletal myogenesis<ref>PMID:28733670</ref>.  For detalis on BRD3 see [[Human bromodomain containing protein 3]]
*'''BRD7''' promotes colorectal cancer by regulating the ubiquitin-proteasome-dependent stabilisation of c-Myc protein<ref>PMID:34109174</ref>.
*'''BRD9''' has a role in activation of interferon-stimulated genes<ref>PMID:34983841</ref>.


== Disease ==
== Disease ==


Dysfunction of BRD is involved in cancer, inflammation and multiple sclerosis.
Dysfunction of BRD is involved in cancer, inflammation, obesity and multiple sclerosis<ref>PMID:22722403</ref>.  BRD4 translocations are detected in NUT midline carcinoma and a variety of BRD4 inhibitors are clinically tested at the present<ref>PMID:18552174</ref>.
 
== Relevance ==


== Structural highlights ==
== Structural highlights ==


</StructureSection>
<scene name='72/724778/Cv/4'>BRD4 bromodomain 1 inhibitors bind to the acetyl-binding pocket</scene><ref>PMID:18552174</ref>. Water molecules are shown as red spheres.
== 3D Structures of bromodomain-containing protein ==
 
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|


*Bromodomain-containing protein 1
**[[3lyi]] – hBRD1 PWWP domain - human<br />
**[[2ku3]] – hBRD1 PHD1 zinc finger domain - NMR<br />
**[[2lq6]] – hBRD1 PHD2 zinc finger domain (mutant) - NMR<br />
**[[3l43]] – histone H3.3 N-terminal/hBRD1 PHD1 zinc finger domain - NMR<br />
**[[3rcw]] – hBRD1 bromodomain <br />
**[[5ame]] – hBRD1 bromodomain+PHD (mutant) + piperazine derivative<br />
**[[5amf]] – hBRD1 bromodomain+PHD (mutant) + indazole derivative<br />
**[[5fg6]] – hBRD1 bromodomain+PHD + probe<br />
**[[4z02]] – hBRD1 residues 925-1049 + quinoline derivative<br />
*Bromodomain-containing protein 2
**[[1x0j]], [[2dvv]] – hBRD2 N-terminal bromodomain <br />
**[[5hel]], [[5hem]], [[5hen]], [[5hfq]] – hBRD2 N-terminal bromodomain (mutant)<br />
**[[2g4a]] – hBRD2 residues 1-116 - NMR<br />
**[[4qeu]], [[5dfb]] – hBRD2 bromodomain 2 (mutant)<br />
*Bromodomain-containing protein 2 complex
**[[2dvq]], [[2dvr]], [[2dvs]], [[2e3k]] – hBRD2 N-terminal bromodomain + histone H4 peptide<br />
**[[3oni]] – hBRD2 residues 224-335 + inhibitor<br />
**[[3aqa]], [[2ydw]], [[2yek]], [[4a9e]], [[4a9f]], [[4a9h]], [[4a9i]], [[4a9j]], [[4a9m]], [[4a9n]], [[4a9o]], [[4alh]], [[4akn]], [[4alg]], [[4uyf]], [[4uyg]], [[4uyh]] – hBRD2 N-terminal bromodomain + inhibitor<br />
**[[4mr5]], [[4mr6]], [[4j1p]] – hBRD2 bromodomain 2 + inhibitor<br />
**[[5bt5]] – hBRD2 bromodomain 2 + probe<br />
**[[4qev]], [[4qew]] – hBRD2 bromodomain 2 (mutant) + probe<br />
**[[5dfc]], [[5dfd]] – hBRD2 bromodomain 2 (mutant) + ligand<br />
*Bromodomain-containing protein 3
**[[2nxb]] – hBRD3 bromodomain 1<br />
**[[2yw5]] – hBRD3 bromodomain 1 - NMR<br />
**[[3s91]], [[3s92]] – hBRD3 bromodomain 1 + inhibitor<br />
**[[2l5e]] – mBRD3 bromodomain 1 + GATA-1 C-terminal – mouse - NMR<br />
**[[2oo1]] – hBRD3 bromodomain 2<br />
**[[2e7n]] – hBRD3 bromodomain 2 - NMR<br />
**[[5hfr]] – hBRD3 bromodomain 2 (mutant)<br />
*Bromodomain-containing protein 4
**[[2oss]], [[4j3i]], [[4lyi]] – hBRD4 bromodomain 1<br />
**[[2ouo]] – hBRD4 bromodomain 2<br />
**[[2i8n]] – hBRD4 bromodomain 2 - NMR<br />
**[[3jvj]] – mBRD4 bromodomain 1<br />
**[[2dww]], [[3jvl]], [[3jvm]] – mBRD4 bromodomain 2<br />
**[[2jns]] – mBRD4 ET domain - NMR<br />
*Bromodomain-containing protein 4 bromodomain 1 complex
**[[3jvk]], [[3muk]], [[3mul]] – mBRD4 bromodomain 1 + histone H3.3 peptide<br />
**[[3uvw]], [[3uvy]], [[3uvx]], [[3uw9]] – hBRD4 bromodomain 1 + histone H4 peptide<br />
**[[4kv1]] – hBRD4 bromodomain 1 + Rel peptide<br />
**[[3mxf]] – mBRD4 bromodomain 1 + inhibitor<br />
**[[3p5o]], [[2yel]], [[3zyu]], [[3u5j]], [[3u5k]], [[4a9l]], [[4e96]], [[4f3i]], [[4hxk]], [[4hxl]], [[4hxm]], [[4hxn]], [[4hxo]], [[4hxp]], [[4hxr]], [[4hxs]], [[4lr6]], [[4lrg]], [[3svf]], [[3svg]], [[4gpj]], [[4hbv]], [[4hbw]], [[4hbx]], [[4hby]], [[4don]], [[4j0r]], [[4j0s]], [[4bw1]], [[4bw2]], [[4bw3]], [[4bw4]], [[4men]], [[4meo]], [[4mep]], [[4meq]], [[4bjx]], [[4c66]], [[4c67]], [[4ioo]], [[4ioq]], [[4ior]], [[4mr3]], [[4mr4]], [[4nqm]], [[4nr8]], [[4cfk]], [[4cfl]], [[4lyw]], [[4ogi]], [[4ogj]], [[4o70]], [[4o71]], [[4o72]], [[4o74]], [[4o75]], [[4o76]], [[4o77]], [[4o78]], [[4o7a]], [[4o7b]], [[4o7c]], [[4o7e]], [[4o7f]], [[4ps5]], [[4nuc]], [[4nue]], [[4nud]], [[4pce]], [[4pci]], [[4uyd]], [[4qzs]], [[4wiv]], [[4cl9]], [[4clb]], [[4xy9]], [[4xya]], [[4z1q]], [[4z1s]], [[4uix]], [[4uiy]], [[4uiz]], [[4qr3]], [[4qr4]], [[4qr5]], [[5bt4]], [[5a5s]], [[5a85]], [[5acy]], [[4x2i]], [[4zc9]], [[5fbx]], [[4yh3]], [[4yh4]], [[5coi]], [[5cp5]], [[5cpe]], [[5cqt]], [[5crm]], [[5crz]], [[5cs8]], [[5ctl]], [[5cy9]], [[5d0c]], [[5dx4]], [[4lzs]], [[5d24]], [[5d25]], [[5d26]], [[5d3h]], [[5d3j]], [[5d3l]], [[5d3n]], [[5d3p]], [[5d3r]], [[5d3s]], [[5d3t]], [[5egu]], [[5ei4]], [[5eis]], [[5hls]], [[5hm0]] – hBRD4 bromodomain 1 + inhibitor<br />
**[[4lys]], [[4lzr]] – hBRD4 bromodomain 1 + colchiceine<br />
**[[4qb3]] – hBRD4 bromodomain 1 + olinone<br />
**[[4whw]] – hBRD4 bromodomain 1 + probe<br />
*Bromodomain-containing protein 4 bromodomain 2 complex
**[[2yem]], [[4z93]] – hBRD4 bromodomain 2 + inhibitor<br />
**[[2lsp]] – hBRD4 bromodomain 2 + Nf-Kb peptide<br />
**[[4kv4]] – hBRD4 bromodomain 2 + Rel peptide<br />
**[[2mjv]] – hBRD4 bromodomain 2 + Twist peptide<br />
*Bromodomain-containing protein 9
**[[3hme]] – hBRD9 bromodomain <br />
**[[4nqn]], [[4xy8]], [[4z6h]], [[4z6i]], [[5e9v]] – hBRD9 bromodomain + inhibitor<br />
**[[4yy4]] – hBRD9 bromodomain + DMSO<br />
**[[4yy6]], [[4yyd]], [[4yyg]], [[4yyh]], [[4yyj]], [[4yyk]] – hBRD9 bromodomain + histone H4 peptide<br />
**[[4uit]], [[4uiu]], [[4uiv]], [[4uiw]] – hBRD9 N-terminal bromodomain + inhibitor<br />
}}


== 3D Structures of bromodomain-containing protein ==
[[Bromodomain-containing protein 3D structures]]


</StructureSection>


== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman
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