PDBsum entry 2i7k

Transcription

PDB id: 2i7k

Contents

Protein chain

117 a.a. *

* Residue conservation analysis

PDB id:

2i7k

Name:

Transcription

Title:

Solution structure of the bromodomain of human brd7 protein

Structure:

Bromodomain-containing protein 7. Chain: a. Fragment: bromodomain. Synonym: 75 kda bromodomain protein, protein celtix-1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Strain: brain. Gene: brd7. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

H.Sun,J.Liu,J.Zhang,H.Huang,J.Wu,Y.Shi

Key ref:

H.Sun et al. (2007). Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4. Biochem Biophys Res Commun, 358, 435-441. PubMed id: 17498659

Date:

31-Aug-06 Release date: 10-Jul-07

Protein chain

Q9NPI1  (BRD7_HUMAN) -  Bromodomain-containing protein 7 from Homo sapiens

Seq: 651 a.a.

Struc: 117 a.a.*

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

Biochem Biophys Res Commun 358:435-441 (2007)

PubMed id: 17498659

Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4.

H.Sun, J.Liu, J.Zhang, W.Shen, H.Huang, C.Xu, H.Dai, J.Wu, Y.Shi.

ABSTRACT

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.