Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase
نویسندگان
چکیده
منابع مشابه
Resistance to a protein farnesyltransferase inhibitor in Plasmodium falciparum.
The post-translational farnesylation of proteins serves to anchor a subset of intracellular proteins to membranes in eukaryotic organisms and also promotes protein-protein interactions. Inhibition of protein farnesyltransferase (PFT) is lethal to the pathogenic protozoa Plasmodium falciparum. Parasites were isolated that were resistant to BMS-388891, a tetrahydroquinoline (THQ) PFT inhibitor. R...
متن کاملProtein farnesyltransferase and protein prenylation in Plasmodium falciparum.
Comparison of the malaria parasite and mammalian protein prenyltransferases and their cellular substrates is important for establishing this enzyme as a target for developing antimalarial agents. Nineteen heptapeptides differing only in their carboxyl-terminal amino acid were tested as alternative substrates of partially purified Plasmodium falciparum protein farnesyltransferase. Only NRSCAIM a...
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Atovaquone is the major active component of the new antimalarial drug Malarone. Considerable evidence suggests that malaria parasites become resistant to atovaquone quickly if atovaquone is used as a sole agent. The mechanism by which the parasite develops resistance to atovaquone is not yet fully understood. Atovaquone has been shown to inhibit the cytochrome bc(1) (CYT bc(1)) complex of the e...
متن کاملRESISTANCE OF PLASMODIUM FALCIPARUM TO CHLOROQUINE IN SOUTH EASTERN IRAN
In vivo and in vitro assessments of the response of P. falciparum to chloroquine using WHO standard kits and techniques were carried out in I ran Shahr, Sistan and Baluchestan province of Iran in 1985. In the in vivo assessment, 24 malaria patients treated with chloroquine (25mg/kg over three days) were followed up for one to four weeks. The mean parasite clearance time was 4.3 days and in...
متن کاملBinding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein.
Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 A resolution crystal structures of a P. falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to...
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ژورنال
عنوان ژورنال: Molecular and Biochemical Parasitology
سال: 2007
ISSN: 0166-6851
DOI: 10.1016/j.molbiopara.2006.11.012