Histone acetyltransferase

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spinqualitylabelsall models Yeast histone acetyltransferase complex with acetyl CoA and Ca+2 ion (green) (PDB entry 1bob) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Disease 4 Structural highlights Function Histone acetyltransferase (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation[1]. Relevance Inhibitors of HAT are potential drugs for inflammatory diseases[2]. Disease Aberrant forms of HAT have been linked to congenital developmental disorders and various forms of cancer[3]. Structural highlights in a of the protein[4]. Water molecules shown as red spheres.

3D Structures of histone acetyltransferase

Updated on 16-May-2019

References

1. ↑ Roth SY, Denu JM, Allis CD. Histone acetyltransferases. Annu Rev Biochem. 2001;70:81-120. PMID:11395403 doi:10.1146/annurev.biochem.70.1.81
2. ↑ Dekker FJ, van den Bosch T, Martin NI. Small molecule inhibitors of histone acetyltransferases and deacetylases are potential drugs for inflammatory diseases. Drug Discov Today. 2014 May;19(5):654-60. doi: 10.1016/j.drudis.2013.11.012. Epub, 2013 Nov 21. PMID:24269836 doi:http://dx.doi.org/10.1016/j.drudis.2013.11.012
3. ↑ Van Beekum O, Kalkhoven E. Aberrant forms of histone acetyltransferases in human disease. Subcell Biochem. 2007;41:233-62. PMID:17484131
4. ↑ Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell. 1998 Aug 21;94(4):427-38. PMID:9727486