Structural highlights
FunctionPublication Abstract from PubMedThe common liver fluke Fasciola hepatica causes an increasing burden on human and animal health, partly because of the spread of drug-resistant isolates. As a consequence, there is considerable interest in developing new drugs to combat liver fluke infections. A group of potential targets is a family of calcium-binding proteins which combine an N-terminal domain with two EF-hand motifs and a C-terminal domain with predicted similarity to dynein light chains (DLC-like domain). The function of these proteins is unknown, although in several species, they have been localised to the tegument, an important structure at the host-parasite interface. Here, we report the X-ray crystal structure of the DLC-like domain of F. hepatica calcium-binding protein 2 (FhCaBP2), solved using single-wavelength anomalous diffraction and refined at 2.3 A resolution in two different crystal forms. The FhCaBP2 DLC-like domain has a structure similar to other DLC domains, with an anti-parallel beta-sheet packed against an alpha-helical hairpin. Like other DLC domains, it dimerises through its beta2-strand, which extends in an arch and forms the fifth strand in an extended beta-sheet of the other monomer. The structure provides molecular details of the dimerisation of FhCaBP2, the first example from this family of parasite proteins. Fasciola hepatica calcium-binding protein FhCaBP2: structure of the dynein light chain-like domain.,Nguyen TH, Thomas CM, Timson DJ, van Raaij MJ Parasitol Res. 2016 Apr 16. PMID:27083189[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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