Sandbox Reserved 654: Difference between revisions

<Structure load='1JM4' size='500' frame='true' align='right' caption='This is a model of the pheylalanine hydroxylase dimer as found in humans. The green ball in within each subunit represents the iron ion in the catalytic domains.' scene='Insert optional scene name here' />

The bromodomain is an evolutionary conserved motif found in chromatin remodeling complexes. It has been identified in over 100 proteins from multiple organisms ranging from unicellular microscopic eukaryotes (e.g., yeast) to humans. The motif is best known for the groundbreaking recent discoveries made to identify it as the only acetyl-lysine binding domain, Dhalluin, C. et al (1999) Nature 399, 491, and to reveal its highly specific ligand selectivity properties. Zeng, L. (2002) FEBS 513:1, 124. Due to these novel characteristics, bromodomains are typically found in proteins responsible for modifications in chromatin structure and the regulation of gene expression, such as histone acetyltransferases (HATs), and the ATPase subunits of chromatin remodeling complexes. There are several families of proteins with bromodomains. One such family is the human transcriptional coactivator p300/CBP-associated factor (PCAF) bromodomain, <ref> sample ref </ref>