Sandbox Reserved 654: Difference between revisions
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== Function == | == Function == | ||
<Structure load='1WUG' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | |||
The hydrophobic pocket formed by the loops is the primary binding site for acetyl-lysine proteins. 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. Once the acetyl-lysine residue makes the initial binding inside the hydrophobic pocket, the ZA and BC loop residues at the entrance of the pocket interact with the amino acids adjacent (+/- 1 or 2) to the already bound acetyl-lysine. Those interactions reinforce binding of the target sequence. Mujtaba, S. et al (2007) Oncogene 26, 5521. Small structural changes in the conformation of the ZA and BC loops result in exposing other residues that are originally buried within the protein to aid in peptide recognition. Mujtaba, S. et al (2002) Mol. Cell 9, 575. | The hydrophobic pocket formed by the loops is the primary binding site for acetyl-lysine proteins. 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. Once the acetyl-lysine residue makes the initial binding inside the hydrophobic pocket, the ZA and BC loop residues at the entrance of the pocket interact with the amino acids adjacent (+/- 1 or 2) to the already bound acetyl-lysine. Those interactions reinforce binding of the target sequence. Mujtaba, S. et al (2007) Oncogene 26, 5521. Small structural changes in the conformation of the ZA and BC loops result in exposing other residues that are originally buried within the protein to aid in peptide recognition. Mujtaba, S. et al (2002) Mol. Cell 9, 575. | ||
