Bromodomain: an acetyl‐lysine binding domain

FEBS Letters

Zeng, Lei¹  Zhou, Ming-Ming¹ 

[1] Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, 1425 Madison Avenue, P.O. Box 1677, New York, NY 10029-6574, USA

关键词: Bromodomain;    Chromatin remodeling;    Histone modification;    Lysine acetylation;    Transcriptional regulation;    HAT;    histone acetyltransferase;    HIV-1;    human immunodeficiency virus type 1;    NMR;    nuclear magnetic resonance;    P/CAF;    p300/CBP-associated factor;   

DOI  :  10.1016/S0014-5793(01)03309-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bromodomains, an extensive family of evolutionarily conserved protein modules originally found in proteins associated with chromatin and in nearly all nuclear histone acetyltransferases, have been recently discovered to function as acetyl-lysine binding domains. More recent structural studies of bromodomain/peptide ligand complexes have enriched our understanding of differences in ligand selectivity of bromodomains. These new findings demonstrate that bromodomain/acetyl-lysine recognition can serve as a pivotal mechanism for regulating protein–protein interactions in numerous cellular processes including chromatin remodeling and transcriptional activation, and reinforce the concept that functional diversity of a conserved protein modular structure is achieved by evolutionary changes of amino acid sequences in the ligand binding site.

【 授权许可】

Unknown