Bromodomains (BRDs) are evolutionarily conserved protein–protein interaction modules that share a bundle of 4 α-helices (αZ, αA, αB and αC) linked to each other by loop segments of variable length (ZA and BC loops). BRDs primarily recognize acetylated Lys residues on histones. However, several BRDs were found to recognize acetylated non-histone proteins. BRD-containing proteins regulate gene expression, alone or as part of larger protein complexes, through chromatin remodelling, histone modification, histone recognition and transcriptional machinery regulation. BRD-containing proteins are frequently deregulated in cancer, and mutations in the BRDs themselves are frequently identified in a variety of cancers. BRD-containing proteins also form part of oncogenic fusion proteins that result from chromosomal rearrangements, being an interesting targets for drug design. Here you can see the crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 protein (PDB code: 7LB0).
#molecularart ... #immolecular ... #bromodomain ... #histone ..: #recognition ... #binding ... #geneexpression ... #regulation ... #cancer ... Rendered with @proteinimaging and finished with @corelphotopaint
#molecularart ... #immolecular ... #bromodomain ... #histone ..: #recognition ... #binding ... #geneexpression ... #regulation ... #cancer ... Rendered with @proteinimaging and finished with @corelphotopaint
