User:James Lignos/Sandbox 1
From Proteopedia
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==Bromodomain of PfBDP1== | ==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 <scene name='10/1078792/Four_left_handed_alpha_helices/1'>four left handed alpha helices</scene>, which is a conserved structural element amongst bromodomains. The core four helix bundle is arranged in two halves connected by the <scene name='10/1078792/Ab_and_bc_loops/2'>AB and BC Loops</scene> | + | 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 <scene name='10/1078792/Four_left_handed_alpha_helices/1'>four left handed alpha helices</scene>, which is a conserved structural element amongst bromodomains. The core four helix bundle is arranged in two halves connected by the <scene name='10/1078792/Ab_and_bc_loops/2'>AB and BC Loops</scene>The first half of the four helical bundle is comprised of the <scene name='10/1078792/Pfbdp1_bromodomain_az_aa/1'>αZ (333–357 aa) and αA (379–389 aa) helices.</scene>. The end of the αZ helix encodes a <scene name='10/1078792/Scene_3/2'>‘HIF’ shelf</scene> 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. |
<Structure load='9HHD' size='350' frame='true' align='right' caption='PDB ID 9HHD. Plasmodium Falciparum Bromodomain Containing protein 1 complexed with bromodomain inhibitor RMM2. MW 16.09 kDa res.325-456 2.69Å' scene='Insert optional scene name here' /> | <Structure load='9HHD' size='350' frame='true' align='right' caption='PDB ID 9HHD. Plasmodium Falciparum Bromodomain Containing protein 1 complexed with bromodomain inhibitor RMM2. MW 16.09 kDa res.325-456 2.69Å' scene='Insert optional scene name here' /> | ||
<StructureSection load='1stp' size='340' side='right' caption='=''> | <StructureSection load='1stp' size='340' side='right' caption='=''> | ||
Revision as of 19:30, 24 April 2025
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.
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