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January 4, 2002FEBS Letters

Bromodomain: an acetyl‐lysine binding domain

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Authors

LZLei ZengLoudi Central HospitalMZMing‐Ming ZhouNantong University

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Implication

Structural analysis reveals bromodomains recognize acetyl-lysine to regulate chromatin remodeling and transcription, highlighting how binding site mutations drive functional diversity.

Key Points

  • To review structural insights into bromodomains as acetyl-lysine recognition domains and determine how sequence variations dictate ligand selectivity.
  • Analyzed structural data from bromodomain and peptide ligand complexes.
  • Evaluated evolutionary conservation and sequence diversity across chromatin-associated proteins and nuclear histone acetyltransferases.
  • Identified bromodomains as conserved functional modules that specifically bind acetyl-lysine residues across chromatin-associated proteins.
  • Demonstrated that evolutionary sequence alterations in ligand binding sites drive functional diversity and regulate essential protein-protein interactions in chromatin remodeling and transcriptional activation.

Cite This Study

Zeng et al. (2002) studied this question.

synapsesocial.com/papers/6984b44b3ee498a9db49a3d5https://doi.org/10.1016/s0014-5793(01)03309-9
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