PDBsum entry 4ioo

DNA binding protein

PDB id

4ioo

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Contents

			Protein chain

					126 a.a.

			Ligands

					EDO ×5


					BAE


					DMS

			Waters ×172

PDB id:

4ioo

Links

Name:

DNA binding protein

Title:

Crystal structure of the first bromodomain of brd4 in complex with n- methyltrimethylacetamide

Structure:

Bromodomain-containing protein 4. Chain: a. Fragment: first bromodomain (unp residues 44-168). Synonym: protein hunk1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: brd4, hunk1. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

1.25Å

R-factor:

0.150

R-free:

0.167

Authors:

G.Lolli,R.Battistutta

Key ref:

G.Lolli and R.Battistutta (2013). Different orientations of low-molecular-weight fragments in the binding pocket of a BRD4 bromodomain. Acta Crystallogr D Biol Crystallogr, 69, 2161-2164. PubMed id: 24100334 DOI: 10.1107/S090744491301994X

Date:

08-Jan-13

Release date:

02-Oct-13

PROCHECK

	Headers

	References

Protein chain

O60885 (BRD4_HUMAN) - Bromodomain-containing protein 4 from Homo sapiens

Seq: Struc:

Seq: Struc:

Seq: Struc:					1362 a.a. 126 a.a.*

Key:

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1107/S090744491301994X	Acta Crystallogr D Biol Crystallogr 69:2161-2164 (2013)
PubMed id: 24100334

Different orientations of low-molecular-weight fragments in the binding pocket of a BRD4 bromodomain.
G.Lolli, R.Battistutta.

ABSTRACT

Bromodomains are involved in the regulation of chromatin architecture and transcription through the recognition of acetylated lysines in histones and other proteins. Many of them are considered to be relevant pharmacological targets for different pathologies. Three crystallographic structures of the N-terminal bromodomain of BRD4 in complex with low-molecular-weight fragments are presented. They show that similar molecules mimicking acetylated lysine bind the bromodomain with different orientations and exploit different interactions. It is also advised to avoid DMSO when searching for low-affinity fragments that interact with bromodomains since DMSO binds in the acetylated lysine-recognition pocket of BRD4.