Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5M3A

Crystal structure of BRD4 BROMODOMAIN 1 IN COMPLEX WITH LIGAND 2

Summary for 5M3A
Entry DOI10.2210/pdb5m3a/pdb
DescriptorBromodomain-containing protein 4, 1,2-ETHANEDIOL, 3-methyl-6-(1-methyl-5-phenoxy-pyrazol-4-yl)-[1,2,4]triazolo[4,3-b]pyridazine, ... (4 entities in total)
Functional Keywordsbromodomain, brd4 bd1, epigenetic, histone reader, transcription
Biological sourceHomo sapiens (Human)
Cellular locationNucleus: O60885
Total number of polymer chains1
Total formula weight15529.84
Authors
Kessler, D.,Mayer, M.,Engelhardt, H.,Wolkerstorfer, B.,Geist, L. (deposition date: 2016-10-14, release date: 2017-09-27, Last modification date: 2024-01-17)
Primary citationGeist, L.,Mayer, M.,Cockcroft, X.L.,Wolkerstorfer, B.,Kessler, D.,Engelhardt, H.,McConnell, D.B.,Konrat, R.
Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and Its Application to Drug Design.
J. Med. Chem., 60:8708-8715, 2017
Cited by
PubMed Abstract: Fragment-based drug design exploits initial screening of low molecular weight compounds and their concomitant affinity improvement. The multitude of possible chemical modifications highlights the necessity to obtain structural information about the binding mode of a fragment. Herein we describe a novel NMR methodology (LOGSY titration) that allows the determination of binding modes of low affinity binders in the protein-ligand interface and reveals suitable ligand positions for the addition of functional groups that either address or substitute protein-bound water, information of utmost importance for drug design. The particular benefit of the methodology and in contrast to conventional ligand-based methods is the independence of the molecular weight of the protein under study. The validity of the novel approach is demonstrated on two ligands interacting with bromodomain 1 of bromodomain containing protein 4, a prominent cancer target in pharmaceutical industry.
PubMed: 28910100
DOI: 10.1021/acs.jmedchem.7b00845
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

238582

数据于2025-07-09公开中

PDB statisticsPDBj update infoContact PDBjnumon