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ACDC Domain
The ''A''P2-''C''oincident ''D''omain mainly at the ''C''arboxy-terminus, or ACDC domain, is a protein domain that occurs in proteins from apicomplexan parasites. It is found exclusively in apicomplexan proteins that also contain AP2 ( Apetala 2-integrase) DNA binding domains (ApiAP2 proteins). In 8 of 9 known examples in the malarial parasite '' Plasmodium falciparum'' it is near the carboxy terminus, with the remaining one being at the amino terminus The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amin .... As yet, beyond its identification and the observation that it occurs only in ApiAP2 proteins, the function of the ACDC domain is unknown. Two proteins with the ACDC domain were found in the nucleus of ''P. falciparum'', as detected by a proteomic method, suggesting a role in nucle ...
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Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer af ...
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Apicomplexan
The Apicomplexa (also called Apicomplexia) are a large phylum of parasitic alveolates. Most of them possess a unique form of organelle that comprises a type of non-photosynthetic plastid called an apicoplast, and an apical complex structure. The organelle is an adaptation that the apicomplexan applies in penetration of a host cell. The Apicomplexa are unicellular and spore-forming. All species are obligate endoparasites of animals, except '' Nephromyces'', a symbiont in marine animals, originally classified as a chytrid fungus. Motile structures such as flagella or pseudopods are present only in certain gamete stages. The Apicomplexa are a diverse group that includes organisms such as the coccidia, gregarines, piroplasms, haemogregarines, and plasmodia. Diseases caused by Apicomplexa include: * Babesiosis (''Babesia'') * Malaria (''Plasmodium'') * Cryptosporidiosis (''Cryptosporidium parvum'') * Cyclosporiasis ('' Cyclospora cayetanensis'') * Cystoisosporiasis ('' Cystoiso ...
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Apetala 2
Apetala 2 (AP2) is a gene and a member of a large family of transcription factors, the AP2/ EREBP family. In '' Arabidopsis thaliana'' AP2 plays a role in the ABC model of flower development. It was originally thought that this family of proteins was plant-specific; however, recent studies have shown that apicomplexans, including the causative agent of malaria, '' Plasmodium falciparum'' encode a related set of transcription factors, called the ApiAP2 family. In the ''A. thaliana'' transcription factor RAV1 the N-terminal AP2 domain binds 5'-CAACA -3' sequence, while the C-terminal The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is ... highly conserved B3 domain binds 5'-CACCTG -3' sequence. Structure and Biological Content of AP2 Through recent studies, Apetala 2 is found ...
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Malarial
Malaria is a mosquito-borne infectious disease that affects humans and other animals. Malaria causes symptoms that typically include fever, tiredness, vomiting, and headaches. In severe cases, it can cause jaundice, seizures, coma, or death. Symptoms usually begin ten to fifteen days after being bitten by an infected mosquito. If not properly treated, people may have recurrences of the disease months later. In those who have recently survived an infection, reinfection usually causes milder symptoms. This partial resistance disappears over months to years if the person has no continuing exposure to malaria. Malaria is caused by single-celled microorganisms of the ''Plasmodium'' group. It is spread exclusively through bites of infected ''Anopheles'' mosquitoes. The mosquito bite introduces the parasites from the mosquito's saliva into a person's blood. The parasites travel to the liver where they mature and reproduce. Five species of ''Plasmodium'' can infect and be sprea ...
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Plasmodium Falciparum
''Plasmodium falciparum'' is a unicellular protozoan parasite of humans, and the deadliest species of ''Plasmodium'' that causes malaria in humans. The parasite is transmitted through the bite of a female '' Anopheles'' mosquito and causes the disease's most dangerous form, falciparum malaria. It is responsible for around 50% of all malaria cases. ''P. falciparum'' is therefore regarded as the deadliest parasite in humans. It is also associated with the development of blood cancer (Burkitt's lymphoma) and is classified as a Group 2A (probable) carcinogen. The species originated from the malarial parasite ''Laverania'' found in gorillas, around 10,000 years ago. Alphonse Laveran was the first to identify the parasite in 1880, and named it ''Oscillaria malariae''. Ronald Ross discovered its transmission by mosquito in 1897. Giovanni Battista Grassi elucidated the complete transmission from a female anopheline mosquito to humans in 1898. In 1897, William H. Welch created the na ...
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Carboxy Terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus. Chemistry Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an unbound amine group, the N-terminus. Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus. Function C-terminal retention signals While the N-terminus of a protein often conta ...
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Amino Terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that j ...
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