期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 22, 期 15, 页码 4990-4993出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2012.06.032
关键词
Methyltransferase; Plasmodium falciparum; Malaria; Crystallography; Aminoquinolines
资金
- National Institutes of Health [AI-097119]
- American Society of Plant Biologists Summer Undergraduate Research Fellowship
- Washington University Howard Hughes Medical Institute Summer Undergraduate Research Fellowship
- Department of Energy Office of Biological and Environmental Research [DE-AC02-06CH11357]
Phosphoethanolamine N-methyltransferase (PMT) is essential for phospholipid biogenesis in the malarial parasite Plasmodium falciparum. PfPMT catalyzes the triple methylation of phosphoethanolamine to produce phosphocholine, which is then used for phosphatidylcholine synthesis. Here we describe the 2.0 A resolution X-ray crystal structure of PfPMT in complex with amodiaquine. To better characterize inhibition of PfPMT by amodiaquine, we determined the IC50 values of a series of aminoquinolines using a direct radiochemical assay. Both structural and functional analyses provide a possible approach for the development of new small molecule inhibitors of PfPMT. (c) 2012 Elsevier Ltd. All rights reserved.
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