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==Crystal Structure of the first bromodomain of human BRDT in complex with the inhibitor JQ1== | |||
<StructureSection load='4flp' size='340' side='right'caption='[[4flp]], [[Resolution|resolution]] 2.23Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4flp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FLP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JQ1:(6S)-6-(2-TERT-BUTOXY-2-OXOETHYL)-4-(4-CHLOROPHENYL)-2,3,9-TRIMETHYL-6,7-DIHYDROTHIENO[3,2-F][1,2,4]TRIAZOLO[4,3-A][1,4]DIAZEPIN-10-IUM'>JQ1</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | |||
== | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4flp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4flp OCA], [https://pdbe.org/4flp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4flp RCSB], [https://www.ebi.ac.uk/pdbsum/4flp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4flp ProSAT]</span></td></tr> | ||
[[4flp]] is a 2 chain structure with sequence from [ | </table> | ||
== Function == | |||
== | [https://www.uniprot.org/uniprot/BRDT_HUMAN BRDT_HUMAN] Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids. Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin.<ref>PMID:9367677</ref> <ref>PMID:15647849</ref> <ref>PMID:22901802</ref> | ||
< | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith | [[Category: Large Structures]] | ||
[[Category: Bountra | [[Category: Arrowsmith CH]] | ||
[[Category: Bradner | [[Category: Bountra C]] | ||
[[Category: Canning | [[Category: Bradner J]] | ||
[[Category: Canning P]] | |||
[[Category: Edwards | [[Category: Edwards A]] | ||
[[Category: Felletar | [[Category: Felletar I]] | ||
[[Category: Filippakopoulos | [[Category: Filippakopoulos P]] | ||
[[Category: Knapp | [[Category: Knapp S]] | ||
[[Category: Muniz | [[Category: Muniz J]] | ||
[[Category: Picaud | [[Category: Picaud S]] | ||
[[Category: Qi | [[Category: Qi J]] | ||
[[Category: | [[Category: Von Delft F]] | ||
Latest revision as of 18:28, 14 March 2024
Crystal Structure of the first bromodomain of human BRDT in complex with the inhibitor JQ1Crystal Structure of the first bromodomain of human BRDT in complex with the inhibitor JQ1
Structural highlights
FunctionBRDT_HUMAN Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids. Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin.[1] [2] [3] References
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