5vbq
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRDT IN COMPLEX WITH BI2536== | |
| - | + | <StructureSection load='5vbq' size='340' side='right' caption='[[5vbq]], [[Resolution|resolution]] 1.65Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5vbq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VBQ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=R78:4-{[(7R)-8-CYCLOPENTYL-7-ETHYL-5-METHYL-6-OXO-5,6,7,8-TETRAHYDROPTERIDIN-2-YL]AMINO}-3-METHOXY-N-(1-METHYLPIPERIDIN-4-YL)BENZAMIDE'>R78</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vbo|5vbo]], [[5vbp|5vbp]], [[5vbr|5vbr]]</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vbq OCA], [http://pdbe.org/5vbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vbq RCSB], [http://www.ebi.ac.uk/pdbsum/5vbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vbq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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: EMBER, S W]] | ||
| + | [[Category: SCHONBRUNN, E]] | ||
| + | [[Category: ZHU, J Y]] | ||
| + | [[Category: Bromodomain]] | ||
| + | [[Category: Cap]] | ||
| + | [[Category: Hunk1]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Mcap]] | ||
| + | [[Category: Mitotic chromosome associated protein]] | ||
| + | [[Category: Protein binding-inhibitor complex]] | ||
| + | [[Category: Transcription-inhibitor complex]] | ||
Revision as of 05:53, 4 April 2018
CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRDT IN COMPLEX WITH BI2536
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