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Reference: www.mshri.on.ca/pawson/research1.html

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Bromo Domains

Structure

A single bromodomain structure is available from HAT coactivator P/CAF (p300/CBP associated factor).  The structure is an unusual left-handed up-and-down four helix bundle with a left handed twist. A hydrophobic pocket in the bromodomain creates a binding site for the acetylated moiety.  Intermolecular interactions are primarily hydrophobic.

Domain binding and function

Approximately 110 amino acids in length, the bromodomain is found in many chromatin-associated proteins.  Bromodomains have been identified in over 100 proteins from yeast to man.  The bromodomain of P/CAF has been shown to specifically interact with peptides containing acetylated lysine residues, and is the only domain known to bind to this motif.  Recognition of acetyl-lysine is similar to that of acetyl-CoA by histone acetyltransferases.

 

Binding examples

BROMO domain proteins

Binding partner 
P/CAF acetyl-lysine containing
peptides