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Bromodomain of PfBDP1

In 2023, globally, there were an estimated 263 million new malaria cases and 597,000 deaths. Plasmodium falciparum, the causative parasite of malaria, invade red blood cells and consumes hemoglobin, preventing oxygen transport to the heart, resulting in heart failure. Additionally, parasitized RBCs stick to the wall of blood vessels in the heart and brain to evade the immune system, which leads to inflammation and blood vessel blockage to these vital organs thus, it is imperative to understand the essential factors involved in the P. falciparum RBC invasion process to develop therapeutic interventions. Previous research has shown that the P. falciparum Bromodomain Protein 1 (PfBDP1) plays an important role in red blood cell invasion by binding to acetylated chromatin at the promoters of invasion genes, promoting their expression, and knockdown of PfBPD1 strongly reduces expression, and blocks the invasion of RBCs. This suggests that the chromatin binding activity of PfBDP1 plays an important role in regulating the expression of invasion-related genes. The bromodomain of PfBDP1 harbors , which is a conserved structural element amongst bromodomains. The core four helix bundle is arranged in two halves connected by the The first half of the four helical bundle is comprised of the . The end of the αZ helix encodes a that forms the bottom of the binding pocket, and the long and variable ZA loop (358–378 aa) frames one side of the binding pocket before connecting to the αA helix which is a conserved structural feature of the bromodomain binding pocket. The second half of the conserved bromodomain fold is comprised of the that form the other side of the binding pocket. The αB helix and the αC helix are connected by the 3-residue long BC loop, which contains the conserved asparagine residue that is involved in the coordination of the acetyllysine moiety

spinqualitylabelsall models PDB ID 9HHD. Plasmodium Falciparum Bromodomain Containing protein 1 complexed with bromodomain inhibitor RMM2. MW 16.09 kDa res.325-456 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

spinqualitylabelsall models PDB ID 1stp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Binds acetylated lysines at promoters of genes implicated in host cell invasion Disease Relevance Structural highlights This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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