2i7k
From Proteopedia
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==Overview== | ==Overview== | ||
| - | BRD7 is an important protein tightly associated with Nasopharyngeal | + | BRD7 is an important protein tightly associated with Nasopharyngeal carcinoma (NPC). Overexpression of BRD7 inhibits NPC cell growth and cell cycle by transcriptionally regulating the cell cycle related genes. BRD7 contains a bromodomain that is found in many chromatin-associated proteins and in nearly all known nuclear histone acetyltransferases (HATs) and plays an important role in chromatin remodeling and transcriptional activation. Here, we report the solution structure of BRD7 bromodomain determined by NMR spectroscopy, and its binding specificity revealed by NMR titration with several acetylated histone peptides. We find that BRD7 bromodomain contains the typical left-handed four-helix bundle topology, and can bind with weak affinity to lysine-acetylated peptides derived from histone H3 with K9 or K14 acetylated and from histone H4 with K8, K12 or K16 acetylated. Our results show that BRD7 bromodomain lacks inherent binding specificity when binding to histones in vitro. |
==About this Structure== | ==About this Structure== | ||
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[[Category: left-handed four-helix bundle]] | [[Category: left-handed four-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:49:55 2008'' |
Revision as of 15:49, 21 February 2008
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Solution Structure of the Bromodomain of Human BRD7 Protein
Overview
BRD7 is an important protein tightly associated with Nasopharyngeal carcinoma (NPC). Overexpression of BRD7 inhibits NPC cell growth and cell cycle by transcriptionally regulating the cell cycle related genes. BRD7 contains a bromodomain that is found in many chromatin-associated proteins and in nearly all known nuclear histone acetyltransferases (HATs) and plays an important role in chromatin remodeling and transcriptional activation. Here, we report the solution structure of BRD7 bromodomain determined by NMR spectroscopy, and its binding specificity revealed by NMR titration with several acetylated histone peptides. We find that BRD7 bromodomain contains the typical left-handed four-helix bundle topology, and can bind with weak affinity to lysine-acetylated peptides derived from histone H3 with K9 or K14 acetylated and from histone H4 with K8, K12 or K16 acetylated. Our results show that BRD7 bromodomain lacks inherent binding specificity when binding to histones in vitro.
About this Structure
2I7K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4., Sun H, Liu J, Zhang J, Shen W, Huang H, Xu C, Dai H, Wu J, Shi Y, Biochem Biophys Res Commun. 2007 Jun 29;358(2):435-41. Epub 2007 May 2. PMID:17498659
Page seeded by OCA on Thu Feb 21 17:49:55 2008
Categories: Homo sapiens | Single protein | Huang, H. | Liu, J. | Shi, Y. | Sun, H. | Wu, J. | Zhang, J. | Helix | Left-handed four-helix bundle
