Sandbox Reserved 896: Difference between revisions
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The BRD2 protein consists of three domains: C-terminal bromodomain 1 (BD1), bromodomain 2 (BD2), and N-extra-terminal domain. As BD1 plays the primary role in coordinating the N-acetyl-lysine ligand, this domain’s structure is of the most functional importance. | The BRD2 protein consists of three domains: C-terminal bromodomain 1 (BD1), bromodomain 2 (BD2), and N-extra-terminal domain. As BD1 plays the primary role in coordinating the N-acetyl-lysine ligand, this domain’s structure is of the most functional importance. | ||
BD1 Structure | '''BD1 Structure''' | ||
BD1 contains a left-handed alpha-helical bundle formed by four alpha helices: aZ, aA, aB, and aC. | BD1 contains a left-handed alpha-helical bundle formed by four alpha helices: aZ, aA, aB, and aC. | ||
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The hydrophobic core is mostly stabilized by conserved hydrophobic residues and few hydrophilic residues. | The hydrophobic core is mostly stabilized by conserved hydrophobic residues and few hydrophilic residues. | ||
BD1 vs. BD2 Drug Selectivity | '''BD1 vs. BD2 Drug Selectivity''' | ||
Genetic divergence between the structures of ZA and BC loops in BD1 vs. BD2 is what allows selective drug targeting of one bromodomain | Genetic divergence between the structures of ZA and BC loops in BD1 vs. BD2 is what allows selective drug targeting of one bromodomain | ||
