Journal
COMBINATORIAL CHEMISTRY & HIGH THROUGHPUT SCREENING
Volume 8, Issue 1, Pages 5-14Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/1386207053328093
Keywords
adenylosuccinate synthetase; PfAdSS; crystallography; cyclophilin; PfCYP19; dihydrofolate reductase/thymidylate synthase; PfDHFR-TS; enoyl-acyl carrier reductase; PfENR; formylmethionine deformylase; PfPDF; glutathione S-transferase; PfGST; hypoxanthine-guanine-xanthine phosphoribosyltransferase; PfHGXPRT; L-lactate dehydrogenase; PfLDH; malaria; medicines for malaria venture; MMV; Plasmepsin II; PfPNP; plasmepsin IV; PfPMIV; Plasmodium falciparum; protein kinase 5; PfPK5; purine nucleoside phosphorylase; PfPNP; structure-based drug discovery triosphosphate isornerase; PfTPI
Funding
- NIGMS NIH HHS [P50 GM64655] Funding Source: Medline
Ask authors/readers for more resources
X-ray crystallography is a technique which is finding increasing utility in the effort to find new antimalarial drugs. This is in spite of the Serious difficulties Often encountered in obtaining sufficient quantities of protein to crystallize. This review provides an overview of the Plasmodium falciparum proteins which have been crystallized with bound inhibitors and the methodology employed in the heterologous expression of these proteins. Lactate dehydrogenase, plasmepsin II, and triosphosphate isomerase are the most advanced targets of structure-based drug design, but nine other P. falciparum proteins have been crystallized with inhibitors as well, and this is clearly an area which is moving very quickly. Some consideration will also be given to the limitations of structure-based drug discovery with respect to known antimalarial drugs.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available