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Structural insights into acetylated histone ligand recognition by the BDP1 bromodomain of Plasmodium falciparum

Int J Biol Macromol. 2022-10; 
Ajit Kumar Singh, Margaret Phillips, Saleh Alkrimi, Marco Tonelli, Samuel P Boyson, Kiera L Malone, Jay C Nix, Karen C Glass
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Custom Vector Construction … The codon-optimized PfBDP1-BRD (303–488) construct cloned in a pGEX-6P-1 vector with an N terminal GST-tag followed by a precision protease site was obtained from GenScript. … Get A Quote


Plasmodium falciparum requires a two-host system, moving between Anopheles mosquito and humans, to complete its life cycle. To overcome such dynamic growth conditions its histones undergo various post-translational modifications to regulate gene expression. The P. falciparum Bromodomain Protein 1 (PfBDP1) has been shown to interact with acetylated lysine modifications on histone H3 to regulate the expression of invasion-related genes. Here, we investigated the ability of the PfBDP1 bromodomain to interact with acetyllsyine modifications on additional core and variant histones. A crystal structure of the PfBDP1 bromodomain (PfBDP1-BRD) reveals it contains the conserved bromodomain fold, but our comparative analy... More


Bromodomain (BRD), Chromatin reader domains, Epigenetics, Histones, Isothermal Titration Calorimetry (ITC), Malaria, Nuclear Magnetic Resonance (NMR), P. falciparum bromodomain-containing proteins (PfBDPs), Plasmodium falciparum (P. falciparum), Post-translational modifications (PTM), X-ray crystallography