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General background information

Bromodomains are evolutionarily conserved protein modules that specifically recognize acetylated lysine residues on histone tails of the nucleosome. During red-blood-cell-stage infection of Plasmodium falciparum, the parasite undergoes repeated rounds of replication, egress, and invasion. Erythrocyte invasion involves specific interactions between host cell receptors and parasite ligands and coordinated expression of genes specific to this step of the life cycle. Parasite-specific bromodomain protein, PfBDP1, binds to chromatin at transcriptional start sites of invasion-related genes and directly controls their expression. A parasite-specific bromodomain protein, PfBDP1, as shown in figure (4), is essential in malaria parasites. PfBDP1 binds to chromatin at invasion gene promoters. Depletion of PfBDP1 dysregulates invasion gene expression and disrupts invasion. PfBDP1 as a critical activator of the coordinate expression of genes that encode proteins with an essential role in erythrocyte invasion.

Structure Features

PfBDP1 (PF3D7_1033700), is a 55 kDa protein. As shown in Figure below, the domain architecture of P. falciparum bromodomain protein 1 (PfBDP1) contains a single C-terminal bromodomain and a number of ankyrin repeats (in the N-terminal portion of the protein, presumably operating in protein-protein interactions); this architecture appears to be unique to apicomplexan parasites.

Bromodomain Histone Ligand Recognition

PfBDP1 bromodomain can recognize different acetyllysine histone ligands with varying binding affinities. Currently, it is known that PfBDP1 binds to acetylated histone H3, and it predominantly recognizes H3K9ac and H3K14ac^[3]. PfBDP1 was shown to positively regulate transcription of invasion genes by binding to acetylated histone H3.^[4]

Classification

Signaling Protien

Function

PfBDP1 has been shown to be involved in the regulation of invasion-related genes in asexual stage parasites. Also, it appears to be essential for parasite growth^[5].

Sequence alignment

Ligand Interaction Domain

Bromodomain Ligand Interaction

Function

PfBDP1, binds to chromatin at transcriptional start sites of invasion-related genes and directly controls their expression. bromodomain protein (PfBDP1), directly exerts positive regulation of invasion genes and is required for normal erythrocyte invasion.

Conservation

Evolutionary Conservation

Relation To Others

Role in Disease

Medical Important

Malaria is a major public health problem in many developing countries, with the malignant tertian parasite Plasmodium falciparum causing the most malaria-associated mortality.

Relevance

Biological source

Plasmodium falciparum (isolate 3D7)

Total molecular weight

19773.77

Structural highlights

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