Sandbox Reserved 654: Difference between revisions
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== Function == | == Function == | ||
<Structure load='1jm4' size='500' frame='true' align='right' caption='Insert caption here' scene=' | <Structure load='1jm4' size='500' frame='true' align='right' caption='Insert caption here' scene='PCAF bromodomain bound to HIV-1 Tat NMR structure ' /> | ||
Until recently, the function of the bromodomain remained unknown. Its structure and modularity, along with its feature of both N and C termini located together on one end of the protein, suggested that it played a role in protein-protein interactions. It has now been shown that the hydrophobic pocket formed by the loops is the primary binding site for acetyl-lysine proteins, making the bromodomain a functional site for recognition of acetylated lysine residues playing a role in regulation via protein-protein interactions. '''Dhalluin'''. This interaction has been shown via localization and chemical shift experiments that revealed the specific manner with which the bromodomain hydrophobic cavity binds to acetylated lysine residues. | Until recently, the function of the bromodomain remained unknown. Its structure and modularity, along with its feature of both N and C termini located together on one end of the protein, suggested that it played a role in protein-protein interactions. It has now been shown that the hydrophobic pocket formed by the loops is the primary binding site for acetyl-lysine proteins, making the bromodomain a functional site for recognition of acetylated lysine residues playing a role in regulation via protein-protein interactions. '''Dhalluin'''. This interaction has been shown via localization and chemical shift experiments that revealed the specific manner with which the bromodomain hydrophobic cavity binds to acetylated lysine residues. | ||
