Histone acetyltransferase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
- | HAT binds acetyl CoA in a cleft toward the center of the concave surface of the protein<ref>PMID:9727486</ref>. | + | <scene name='46/467281/Cv/5'>HAT binds acetyl CoA</scene> in a <scene name='46/467281/Cv/6'>cleft toward the center of the concave surface</scene> of the protein<ref>PMID:9727486</ref>. Water molecules shown as red spheres. |
</StructureSection> | </StructureSection> | ||
== 3D Structures of histone acetyltransferase == | == 3D Structures of histone acetyltransferase == |
Revision as of 09:44, 30 March 2016
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3D Structures of histone acetyltransferase
Updated on 30-March-2016
References
- ↑ 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
- ↑ 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
- ↑ Van Beekum O, Kalkhoven E. Aberrant forms of histone acetyltransferases in human disease. Subcell Biochem. 2007;41:233-62. PMID:17484131
- ↑ 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