NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35.

ABSTRACT: The emergence of drug-resistant malaria parasites is the major threat to effective malaria control, prompting a search for novel compounds with mechanisms of action that are different from the traditionally used drugs. The immunosuppressive drug FK506 shows an antimalarial activity. The mechanism of the drug action involves the molecular interaction with the parasite target proteins PfFKBP35 and PvFKBP35, which are novel FK506 binding protein family (FKBP) members from Plasmodium falciparum and Plasmodium vivax, respectively. Currently, molecular mechanisms of the FKBP family proteins in the parasites still remain elusive. To understand their functions, here we have determined the structures of the FK506 binding domain of Plasmodium vivax (PvFKBD) in unliganded form by NMR spectroscopy and

SUBMITTER: Alag R 

PROVIDER: S-EPMC2923510 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature