R. Tranter

TL;DR: Encouraging results suggest that further enhancement of these structures may yield candidates suitable for consideration as new therapeutics for the treatment of malaria, and provide strong support for the validity of targeting the Plasmodium glycolytic pathway and LDH in the search for novel anti-malarials.

TL;DR: The crystal structure of the complex between chloroquine and P. falciparum lactate dehydrogenase provides a template from which the quinoline moiety might be modified to develop more efficient inhibitors of the enzyme.

TL;DR: The crystal structure of the minimal DNA-binding domain (DBD) from the HPV 6 E2 protein is presented and it is shown that the HPV6 E2 DBD is structurally more similar to the HPV 18 and bovine papillomavirus type 1 (BPV1) E2 proteins than it is to theHP 16 E2protein.

TL;DR: The expression, kinetic characterisation and crystal structure determination of the LDH from Plasmodium berghei are described, implying the special features previously described for PfLDH may be shared across the Plas modium genus, supporting the universal application of therapeutics targeting this enzyme.

TL;DR: From the three-dimensional structure of β-acrosin, two separate effector sites are evident: proteolytic activity, believed to be important at various stages during fertilization, arises from the trypsin-like active site, and positively charged regions on the surface adjacent to the active site may act as receptors for binding zona pellucida glycoproteins.