2wp2
From Proteopedia
Structure of Brdt bromodomain BD1 bound to a diacetylated histone H4 peptide.
Structural highlights
FunctionBRDT_MOUSE 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] [4] [5] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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Categories: Large Structures | Mus musculus | Curtet S | Gaucher J | Govin J | Hart DJ | Khochbin S | Krijgsveld J | Moriniere J | Mueller CW | Petosa C | Rousseaux S | Sadoul K | Soler-Lopez M | Steuerwald U | Vitte A-L