Summary for 1N72
| Entry DOI | 10.2210/pdb1n72/pdb |
| Descriptor | HISTONE ACETYLTRANSFERASE (1 entity in total) |
| Functional Keywords | histone acetyltransferase bromodomain, 4-helical bundle, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus (By similarity): Q92831 |
| Total number of polymer chains | 1 |
| Total formula weight | 14052.23 |
| Authors | Dhalluin, C.,Carlson, J.E.,Zeng, L.,He, C.,Aggarwal, A.K.,Zhou, M.-M. (deposition date: 2002-11-12, release date: 2002-12-11, Last modification date: 2024-05-22) |
| Primary citation | Dhalluin, C.,Carlson, J.E.,Zeng, L.,He, C.,Aggarwal, A.K.,Zhou, M.-M. Structure and Ligand of a Histone Acetyltransferase Bromodomain Nature, 399:491-496, 1999 Cited by PubMed Abstract: Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription. PubMed: 10365964DOI: 10.1038/20974 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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